Skeletal Muscle: Comparison
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Please note this is a comparison between Version 2 by Lily Guo and Version 1 by Catherine Coirault.

Skeletal muscle is composed of multinucleated, mature muscle cells (myofibers) responsible for contraction, and a resident pool of mononucleated muscle cell precursors (MCPs), that are maintained in a quiescent state in homeostatic conditions. Skeletal muscle is remarkable in its ability to adapt to mechanical constraints, a property referred as muscle plasticity and mediated by both MCPs and myofibers. This review summarizes recent insights into the mechanisms underlying nuclear force transmission in MCPs and myofibers. 

  • mechanotransduction
  • Muscle disorders
  • Nucleus
  • nucleo-cytoplasmic coupling
  • mechanics.
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References

  1. Abmayr, S.M.; Pavlath, G.K. Myoblast fusion: Lessons from flies and mice. Development 2012, 139, 641–656.
  2. Kirby, T.J.; Lammerding, J. Emerging views of the nucleus as a cellular mechanosensor. Nat. Cell Biol. 2018, 20, 373–381.
  3. Ato, S.; Kido, K.; Sase, K.; Fujita, S. Response of resistance exercise-induced muscle protein synthesis and skeletal muscle hypertrophy are not enhanced after disuse muscle atrophy in rat. Front. Physiol. 2020, 11, 469.
  4. Burkholder, T.J. Mechanotransduction in skeletal muscle. Front. Biosci. A J. Virtual Libr. 2007, 12, 174–191.
  5. Masschelein, E.; D’Hulst, G.; Zvick, J.; Hinte, L.; Soro-Arnaiz, I.; Gorski, T.; von Meyenn, F.; Bar-Nur, O.; De Bock, K. Exercise promotes satellite cell contribution to myofibers in a load-dependent manner. Skelet. Muscle 2020, 10, 21.
  6. Aureille, J.; Buffière-Ribot, V.; Harvey, B.E.; Boyault, C.; Pernet, L.; Andersen, T.; Bacola, G.; Balland, M.; Fraboulet, S.; Van Landeghem, L.; et al. Nuclear envelope deformation controls cell cycle progression in response to mechanical force. EMBO Rep. 2019, 20.
  7. Uroz, M.; Wistorf, S.; Serra-Picamal, X.; Conte, V.; Sales-Pardo, M.; Roca-Cusachs, P.; Guimerà, R.; Trepat, X. Regulation of cell cycle progression by cell-cell and cell-matrix forces. Nat. Cell Biol. 2018, 20, 646–654.
  8. Fukuda, S.; Kaneshige, A.; Kaji, T.; Noguchi, Y.-T.; Takemoto, Y.; Zhang, L.; Tsujikawa, K.; Kokubo, H.; Uezumi, A.; Maehara, K.; et al. Sustained expression of HeyL is critical for the proliferation of muscle stem cells in overloaded muscle. eLife 2019, 8, e48284.
  9. Dupont, S.; Morsut, L.; Aragona, M.; Enzo, E.; Giulitti, S.; Cordenonsi, M.; Zanconato, F.; Le Digabel, J.; Forcato, M.; Bicciato, S.; et al. Role of YAP/TAZ in mechanotransduction. Nature 2011, 474, 179–183.
  10. Elosegui-Artola, A.; Andreu, I.; Beedle, A.E.M.; Lezamiz, A.; Uroz, M.; Kosmalska, A.J.; Oria, R.; Kechagia, J.Z.; Rico-Lastres, P.; Le Roux, A.-L.; et al. Force triggers YAP Nuclear entry by regulating transport across nuclear pores. Cell 2017, 171, 1397–1410.e14.
  11. Kumar, A.; Mazzanti, M.; Mistrik, M.; Kosar, M.; Beznoussenko, G.V.; Mironov, A.A.; Garrè, M.; Parazzoli, D.; Shivashankar, G.V.; Mironov, A.A.; et al. ATR Mediates a checkpoint at the nuclear envelope in response to mechanical stress. Cell 2014, 158, 633–646.
  12. Kidiyoor, G.R.; Li, Q.; Bastianello, G.; Bruhn, C.; Giovannetti, I.; Mohamood, A.; Beznoussenko, G.V.; Mironov, A.; Raab, M.; Piel, M.; et al. ATR is essential for preservation of cell mechanics and nuclear integrity during interstitial migration. Nat. Commun. 2020, 11, 4828.
  13. Itano, N.; Okamoto, S.-I.; Zhang, D.; Lipton, S.A.; Ruoslahti, E. Cell spreading controls endoplasmic and nuclear calcium: A physical gene regulation pathway from the cell surface to the nucleus. Proc. Natl. Acad. Sci. USA 2003, 100, 5181–5186.
  14. Enyedi, B.; Jelcic, M.; Niethammer, P. The Cell nucleus serves as a mechanotransducer of tissue damage-induced inflammation. Cell 2016, 165, 1160–1170.
  15. Raab, M.; Gentili, M.; de Belly, H.; Thiam, H.-R.; Vargas, P.; Jimenez, A.J.; Lautenschlaeger, F.; Voituriez, R.; Lennon-Dumenil, A.-M.; Manel, N.; et al. ESCRT III repairs nuclear envelope ruptures during cell migration to limit DNA damage and cell death. Science 2016, 352, 359–362.
  16. Chen, N.Y.; Kim, P.H.; Fong, L.G.; Young, S.G. Nuclear membrane ruptures, cell death, and tissue damage in the setting of nuclear lamin deficiencies. Nucleus 2020, 11, 237–249.
  17. Dahl, K.N.; Ribeiro, A.J.S.; Lammerding, J. Nuclear Shape, mechanics, and mechanotransduction. Circ. Res. 2008, 102, 1307–1318.
  18. Janota, C.S.; Calero-Cuenca, F.J.; Gomes, E.R. The role of the cell nucleus in mechanotransduction. Curr. Opin. Cell Biol. 2020, 63, 204–211.
  19. Enyedi, B.; Niethammer, P. Nuclear membrane stretch and its role in mechanotransduction. Nucleus 2017, 8, 156–161.
  20. Stephens, A.D.; Banigan, E.J.; Adam, S.A.; Goldman, R.D.; Marko, J.F. Chromatin and lamin A determine two different mechanical response regimes of the cell nucleus. Mol. Biol. Cell 2017, 28, 1984–1996.
  21. Stephens, A.D.; Banigan, E.J.; Marko, J.F. Separate roles for chromatin and lamins in nuclear mechanics. Nucleus 2018, 9, 119–124.
  22. Nava, M.M.; Miroshnikova, Y.A.; Biggs, L.C.; Whitefield, D.B.; Metge, F.; Boucas, J.; Vihinen, H.; Jokitalo, E.; Li, X.; García Arcos, J.M.; et al. Heterochromatin-Driven nuclear softening protects the genome against mechanical stress-induced damage. Cell 2020, 181, 800–817.e22.
  23. Stephens, A.D.; Banigan, E.J.; Marko, J.F. Chromatin’s physical properties shape the nucleus and its functions. Curr. Opin. Cell Biol. 2019, 58, 76–84.
  24. Flück, M.; Hoppeler, H. Molecular basis of skeletal muscle plasticity—From gene to form and function. Rev. Physiol. Biochem. Pharmacol. 2003, 146, 159–216.
  25. Martino, F.; Perestrelo, A.R.; Vinarský, V.; Pagliari, S.; Forte, G. Cellular mechanotransduction: From tension to function. Front. Physiol. 2018, 9, 824.
  26. Essawy, N.; Samson, C.; Petitalot, A.; Moog, S.; Bigot, A.; Herrada, I.; Marcelot, A.; Arteni, A.-A.; Coirault, C.; Zinn-Justin, S. An emerin LEM-domain mutation Impairs cell response to mechanical stress. Cells 2019, 8, 570.
  27. Roman, W.; Martins, J.P.; Carvalho, F.A.; Voituriez, R.; Abella, J.V.G.; Santos, N.C.; Cadot, B.; Way, M.; Gomes, E.R. Myofibril contraction and crosslinking drive nuclear movement to the periphery of skeletal muscle. Nat. Cell Biol. 2017, 19, 1189–1201.
  28. Fischer, M.; Rikeit, P.; Knaus, P.; Coirault, C. YAP-mediated mechanotransduction in skeletal muscle. Front. Physiol. 2016, 7.
  29. Owens, D.J.; Fischer, M.; Jabre, S.; Moog, S.; Mamchaoui, K.; Butler-Browne, G.; Coirault, C. Lamin Mutations cause increased YAP Nuclear entry in muscle stem cells. Cells 2020, 9, 816.
  30. Jorgenson, K.W.; Phillips, S.M.; Hornberger, T.A. Identifying the Structural adaptations that drive the mechanical load-induced growth of skeletal muscle: A Scoping review. Cells 2020, 9, 1658.
  31. Owens, D.J.; Messeant, J.; Moog, S.; Viggars, M.; Ferry, A.; Mamchaoui, K.; Lacene, E.; Romero, N.; Brull, A.; Bonne, G.; et al. Lamin-Related congenital muscular dystrophy alters mechanical signaling and skeletal muscle growth. Int. J. Mol. Sci. 2020, 22, 306.
  32. D’Alessandro, M.; Hnia, K.; Gache, V.; Koch, C.; Gavriilidis, C.; Rodriguez, D.; Nicot, A.-S.; Romero, N.B.; Schwab, Y.; Gomes, E.; et al. Amphiphysin 2 Orchestrates nucleus positioning and shape by linking the nuclear envelope to the actin and microtubule cytoskeleton. Dev. Cell 2015, 35, 186–198.
  33. Kim, J.-K.; Louhghalam, A.; Lee, G.; Schafer, B.W.; Wirtz, D.; Kim, D.-H. Nuclear lamin A/C harnesses the perinuclear apical actin cables to protect nuclear morphology. Nat. Commun. 2017, 8, 2123.
  34. Heo, S.-J.; Driscoll, T.P.; Thorpe, S.D.; Nerurkar, N.L.; Baker, B.M.; Yang, M.T.; Chen, C.S.; Lee, D.A.; Mauck, R.L. Differentiation alters stem cell nuclear architecture, mechanics, and mechano-sensitivity. eLife 2016, 5, e18207.
  35. Onuh, J.O.; Qiu, H. Serum response factor-cofactor interactions and their implications in disease. FEBS J. 2020.
  36. Watt, K.I.; Goodman, C.A.; Hornberger, T.A.; Gregorevic, P. The Hippo signaling pathway in the regulation of skeletal muscle mass and function. Exerc. Sport Sci. Rev. 2018, 46, 92–96.
  37. Gnimassou, O.; Francaux, M.; Deldicque, L. Hippo pathway and skeletal muscle mass regulation in mammals: A controversial relationship. Front. Physiol. 2017, 8, 190.
  38. Gabriel, B.M.; Hamilton, D.L.; Tremblay, A.M.; Wackerhage, H. The Hippo signal transduction network for exercise physiologists. J. Appl. Physiol. 2016, 120, 1105–1117.
  39. Maniotis, A.J.; Chen, C.S.; Ingber, D.E. Demonstration of mechanical connections between integrins, cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure. Proc. Natl. Acad. Sci. USA 1997, 94, 849–854.
  40. Wang, N.; Tytell, J.D.; Ingber, D.E. Mechanotransduction at a distance: Mechanically coupling the extracellular matrix with the nucleus. Nat. Rev. Mol. Cell Biol. 2009, 10, 75–82.
  41. Zhang, J.; Alisafaei, F.; Nikolić, M.; Nou, X.A.; Kim, H.; Shenoy, V.B.; Scarcelli, G. Nuclear mechanics within intact cells Is regulated by cytoskeletal network and internal nanostructures. Small 2020, 16, 1907688.
  42. Ramdas, N.M.; Shivashankar, G.V. Cytoskeletal Control of nuclear morphology and chromatin organization. J. Mol. Biol. 2015, 427, 695–706.
  43. Haque, F.; Mazzeo, D.; Patel, J.T.; Smallwood, D.T.; Ellis, J.A.; Shanahan, C.M.; Shackleton, S. Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes. J. Biol. Chem. 2010, 285, 3487–3498.
  44. Crisp, M.; Burke, B. The nuclear envelope as an integrator of nuclear and cytoplasmic architecture. FEBS Lett. 2008, 582, 2023–2032.
  45. Crisp, M.; Liu, Q.; Roux, K.; Rattner, J.B.; Shanahan, C.; Burke, B.; Stahl, P.D.; Hodzic, D. Coupling of the nucleus and cytoplasm: Role of the LINC complex. J. Cell Biol. 2006, 172, 41–53.
  46. Ingber, D.E. Cellular mechanotransduction: Putting all the pieces together again. FASEB J. 2006, 20, 811–827.
  47. Khatau, S.B.; Hale, C.M.; Stewart-Hutchinson, P.J.; Patel, M.S.; Stewart, C.L.; Searson, P.C.; Hodzic, D.; Wirtz, D. A perinuclear actin cap regulates nuclear shape. Proc. Natl. Acad. Sci. USA 2009, 106, 19017–19022.
  48. Luxton, G.W.G.; Gomes, E.R.; Folker, E.S.; Vintinner, E.; Gundersen, G.G. Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement. Science 2010, 329, 956–959.
  49. Kim, D.-H.; Chambliss, A.B.; Wirtz, D. The multi-faceted role of the actin cap in cellular mechanosensation and mechanotransduction. Soft Matter 2013, 9, 5516.
  50. Chambliss, A.B.; Khatau, S.B.; Erdenberger, N.; Robinson, D.K.; Hodzic, D.; Longmore, G.D.; Wirtz, D. The LINC-anchored actin cap connects the extracellular milieu to the nucleus for ultrafast mechanotransduction. Sci. Rep. 2013, 3, 1087.
  51. Neelam, S.; Chancellor, T.J.; Li, Y.; Nickerson, J.A.; Roux, K.J.; Dickinson, R.B.; Lele, T.P. Direct force probe reveals the mechanics of nuclear homeostasis in the mammalian cell. Proc. Natl. Acad. Sci. USA 2015, 112, 5720–5725.
  52. Shiu, J.-Y.; Aires, L.; Lin, Z.; Vogel, V. Nanopillar force measurements reveal actin-cap-mediated YAP mechanotransduction. Nat. Cell Biol. 2018, 20, 262–271.
  53. Khatau, S.B.; Kusuma, S.; Hanjaya-Putra, D.; Mali, P.; Cheng, L.; Lee, J.S.H.; Gerecht, S.; Wirtz, D. The differential formation of the LINC-Mediated perinuclear actin cap in pluripotent and somatic cells. PLoS ONE 2012, 7, e36689.
  54. Cadot, B.; Gache, V.; Gomes, E.R. Moving and positioning the nucleus in skeletal muscle—One step at a time. Nucleus 2015, 6, 373–381.
  55. Falcone, S.; Roman, W.; Hnia, K.; Gache, V.; Didier, N.; Lainé, J.; Auradé, F.; Marty, I.; Nishino, I.; Charlet-Berguerand, N.; et al. N-WASP is required for Amphiphysin-2/BIN 1-dependent nuclear positioning and triad organization in skeletal muscle and is involved in the pathophysiology of centronuclear myopathy. EMBO Mol. Med. 2014, 6, 1455–1475.
  56. Lloyd, C.M.; Berendse, M.; Lloyd, D.G.; Schevzov, G.; Grounds, M.D. A novel role for non-muscle γ-actin in skeletal muscle sarcomere assembly. Exp. Cell Res. 2004, 297, 82–96.
  57. Sanger, J.W.; Kang, S.; Siebrands, C.C.; Freeman, N.; Du, A.; Wang, J.; Stout, A.L.; Sanger, J.M. How to build a myofibril. J. Muscle Res. Cell Motil. 2006, 26, 343–354.
  58. Hotulainen, P.; Lappalainen, P. Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J. Cell Biol. 2006, 173, 383–394.
  59. Bains, W.; Ponte, P.; Blau, H.; Kedes, L. Cardiac actin is the major actin gene product in skeletal muscle cell differentiation in vitro. Mol. Cell. Biol. 1984, 4, 1449–1453.
  60. Lin, J.J.; Lin, J.L. Assembly of different isoforms of actin and tropomyosin into the skeletal tropomyosin-enriched microfilaments during differentiation of muscle cells in vitro. J. Cell Biol. 1986, 103, 2173–2183.
  61. Otey, C.A.; Kalnoski, M.H.; Bulinski, J.C. Immunolocalization of muscle and nonmuscle isoforms of actin in myogenic cells and adult skeletal muscle. Cell Motil. Cytoskelet. 1988, 9, 337–348.
  62. Craig, S.W.; Pardo, J.V. Gamma actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites. Cell Motil. 1983, 3, 449–462.
  63. Rybakova, I.N.; Patel, J.R.; Ervasti, J.M. The Dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J. Cell Biol. 2000, 150, 1209–1214.
  64. Ervasti, J.M. Costameres: The Achilles’ heel of Herculean muscle. J. Biol. Chem. 2003, 278, 13591–13594.
  65. Pegoraro, A.F.; Janmey, P.; Weitz, D.A. Mechanical properties of the cytoskeleton and cells. Cold Spring Harb. Perspect. Biol. 2017, 9, a022038.
  66. Musa, H.; Orton, C.; Morrison, E.E.; Peckham, M. Microtubule assembly in cultured myoblasts and myotubes following nocodazole induced microtubule depolymerisation. J. Muscle Res. Cell Motil. 2003, 24, 301–308.
  67. Becker, R.; Leone, M.; Engel, F. Microtubule Organization in striated muscle cells. Cells 2020, 9, 1395.
  68. Chang, W.; Worman, H.J.; Gundersen, G.G. Accessorizing and anchoring the LINC complex for multifunctionality. J. Cell Biol. 2015, 208, 11–22.
  69. Webster, M.; Witkin, K.L.; Cohen-Fix, O. Sizing up the nucleus: Nuclear shape, size and nuclear-envelope assembly. J. Cell Sci. 2009, 122, 1477–1486.
  70. Starr, D.A. Muscle development: Nucleating Microtubules at the nuclear envelope. Curr. Biol. 2017, 27, R1071–R1073.
  71. Srsen, V.; Fant, X.; Heald, R.; Rabouille, C.; Merdes, A. Centrosome proteins form an insoluble perinuclear matrix during muscle cell differentiation. BMC Cell Biol. 2009, 10, 28.
  72. Warren, R.H. Microtubular organization in elongating myogenic cells. J. Cell Biol. 1974, 63, 550–566.
  73. Pizon, V.; Gerbal, F.; Diaz, C.C.; Karsenti, E. Microtubule-dependent transport and organization of sarcomeric myosin during skeletal muscle differentiation. EMBO J. 2005, 24, 3781–3792.
  74. Wang, S.; Reuveny, A.; Volk, T. Nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and EB1. J. Cell Biol. 2015, 209, 529–538.
  75. Mian, I.; Pierre-Louis, W.S.; Dole, N.; Gilberti, R.M.; Dodge-Kafka, K.; Tirnauer, J.S. LKB1 Destabilizes microtubules in myoblasts and Contributes to myoblast differentiation. PLoS ONE 2012, 7, e31583.
  76. Gundersen, G.G.; Khawaja, S.; Bulinski, J.C. Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiation. J. Cell Biol. 1989, 109, 2275–2288.
  77. Gimpel, P.; Lee, Y.L.; Sobota, R.M.; Calvi, A.; Koullourou, V.; Patel, R.; Mamchaoui, K.; Nédélec, F.; Shackleton, S.; Schmoranzer, J.; et al. Nesprin-1α-dependent microtubule nucleation from the nuclear envelope via Akap450 is necessary for nuclear positioning in muscle cells. Curr. Biol. 2017, 27, 2999–3009.e9.
  78. Block, J.; Schroeder, V.; Pawelzyk, P.; Willenbacher, N.; Köster, S. Physical properties of cytoplasmic intermediate filaments. Biochimica et Biophysica Acta (BBA) Mol. Cell Res. 2015, 1853, 3053–3064.
  79. Fudge, D.S.; Gardner, K.H.; Forsyth, V.T.; Riekel, C.; Gosline, J.M. The mechanical properties of hydrated intermediate filaments: Insights from hagfish slime threads. Biophys. J. 2003, 85, 2015–2027.
  80. Kreplak, L.; Bär, H.; Leterrier, J.F.; Herrmann, H.; Aebi, U. Exploring the mechanical behavior of single intermediate filaments. J. Mol. Biol. 2005, 354, 569–577.
  81. Wagner, O.I.; Rammensee, S.; Korde, N.; Wen, Q.; Leterrier, J.-F.; Janmey, P.A. Softness, strength and self-repair in intermediate filament networks. Exp. Cell Res. 2007, 313, 2228–2235.
  82. Kim, S.; Coulombe, P.A. Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev. 2007, 21, 1581–1597.
  83. Block, J.; Witt, H.; Candelli, A.; Peterman, E.J.G.; Wuite, G.J.L.; Janshoff, A.; Köster, S. Nonlinear loading-rate-dependent force response of individual vimentin intermediate filaments to applied strain. Phys. Rev. Lett. 2017, 118, 048101.
  84. Lorenz, C.; Forsting, J.; Schepers, A.V.; Kraxner, J.; Bauch, S.; Witt, H.; Klumpp, S.; Köster, S. Lateral Subunit coupling determines intermediate filament mechanics. Phys. Rev. Lett. 2019, 123, 188102.
  85. Smoler, M.; Coceano, G.; Testa, I.; Bruno, L.; Levi, V. Apparent stiffness of vimentin intermediate filaments in living cells and its relation with other cytoskeletal polymers. Biochimica et Biophysica Acta (BBA) Mol. Cell Res. 2020, 1867, 118726.
  86. Lammerding, J.; Fong, L.G.; Ji, J.Y.; Reue, K.; Stewart, C.L.; Young, S.G.; Lee, R.T. Lamins A and C but Not Lamin B1 Regulate Nuclear Mechanics. J. Biol. Chem. 2006, 281, 25768–25780.
  87. Patteson, A.E.; Vahabikashi, A.; Pogoda, K.; Adam, S.A.; Mandal, K.; Kittisopikul, M.; Sivagurunathan, S.; Goldman, A.; Goldman, R.D.; Janmey, P.A. Vimentin protects cells against nuclear rupture and DNA damage during migration. J. Cell Biol. 2019, 218, 4079–4092.
  88. Hu, J.; Li, Y.; Hao, Y.; Zheng, T.; Gupta, S.K.; Parada, G.A.; Wu, H.; Lin, S.; Wang, S.; Zhao, X.; et al. High stretchability, strength, and toughness of living cells enabled by hyperelastic vimentin intermediate filaments. Proc. Natl. Acad. Sci. USA 2019, 116, 17175–17180.
  89. Kreplak, L.; Herrmann, H.; Aebi, U. Tensile properties of single desmin intermediate filaments. Biophys. J. 2008, 94, 2790–2799.
  90. Banwell, B.L. Intermediate filament-related myopathies. Pediatric Neurol. 2001, 24, 257–263.
  91. Paulin, D.; Huet, A.; Khanamyrian, L.; Xue, Z. Desminopathies in muscle disease. J. Pathol. 2004, 204, 418–427.
  92. Paulin, D.; Hovhannisyan, Y.; Kasakyan, S.; Agbulut, O.; Li, Z.; Xue, Z. Synemin-related skeletal and cardiac myopathies: An overview of pathogenic variants. Am. J. Physiol. Cell Physiol. 2020, 318, C709–C718.
  93. Capetanaki, Y.; Bloch, R.J.; Kouloumenta, A.; Mavroidis, M.; Psarras, S. Muscle intermediate filaments and their links to membranes and membranous organelles. Exp. Cell Res. 2007, 313, 2063–2076.
  94. Sejersen, T.; Lendahl, U. Transient expression of the intermediate filament nestin during skeletal muscle development. J. Cell Sci. 1993, 106, 1291–1300.
  95. Lazarides, E.; Hubbard, B.D. Immunological characterization of the subunit of the 100 A filaments from muscle cells. Proc. Natl. Acad. Sci. USA 1976, 73, 4344–4348.
  96. Mermelstein, C.S.; Andrade, L.R.; Portilho, D.M.; Costa, M.L. Desmin filaments are stably associated with the outer nuclear surface in chick myoblasts. Cell Tissue Res. 2006, 323, 351–357.
  97. Wilhelmsen, K.; Litjens, S.H.; Kuikman, I.; Tshimbalanga, N.; Janssen, H.; van den Bout, I.; Raymond, K.; Sonnenberg, A. Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J. Cell Biol. 2005, 171, 799–810.
  98. Lazarides, E. Intermediate filaments as mechanical integrators of cellular space. Nature 1980, 283, 249–256.
  99. Capetanaki, Y. Desmin cytoskeleton A Potential regulator of muscle mitochondrial behavior and function. Trends Cardiovasc. Med. 2002, 12, 339–348.
  100. Reipert, S. Association of mitochondria with plectin and desmin intermediate filaments in striated muscle. Exp. Cell Res. 1999, 252, 479–491.
  101. Winter, D.L.; Paulin, D.; Mericskay, M.; Li, Z. Posttranslational modifications of desmin and their implication in biological processes and pathologies. Histochem. Cell Biol. 2014, 141, 1–16.
  102. Snider, N.T.; Omary, M.B. Post-translational modifications of intermediate filament proteins: Mechanisms and functions. Nat. Rev. Mol. Cell Biol. 2014, 15, 163–177.
  103. Gao, Q.Q.; McNally, E.M. The Dystrophin Complex: Structure, Function, and Implications for Therapy. In Comprehensive Physiology; Terjung, R., Ed.; John Wiley & Sons, Inc.: Hoboken, NJ, USA, 2015; pp. 1223–1239.
  104. Boudriau, S.; Vincent, M.; Côté, C.H.; Rogers, P.A. Cytoskeletal structure of skeletal muscle: Identification of an intricate exosarcomeric microtubule lattice in slow- and fast-twitch muscle fibers. J. Histochem. Cytochem. 1993, 41, 1013–1021.
  105. Wang, K.; Ramirez-Mitchell, R. A network of transverse and longitudinal intermediate filaments is associated with sarcomeres of adult vertebrate skeletal muscle. J. Cell Biol. 1983, 96, 562–570.
  106. Li, Z.; Colucci-Guyon, E.; Pinçon-Raymond, M.; Mericskay, M.; Pournin, S.; Paulin, D.; Babinet, C. Cardiovascular lesions and Skeletal myopathy in mice lacking desmin. Dev. Biol. 1996, 175, 362–366.
  107. Price, M.G. Molecular analysis of intermediate filament cytoskeleton—A putative load-bearing structure. Am. J. Physiol. 1984, 246, H566–H572.
  108. Galou, M.; Gao, J.; Humbert, J.; Mericskay, M.; Li, Z.; Paulin, D.; Vicart, P. The importance of intermediate filaments in the adaptation of tissues to mechanical stress: Evidence from gene knockout studies. Biol. Cell 1997, 89, 85–97.
  109. Tolstonog, G.V.; Sabasch, M.; Traub, P. Cytoplasmic Intermediate filaments are stably associated with nuclear matrices and potentially modulate their DNA-binding function. DNA Cell Biol. 2002, 21, 213–239.
  110. Boriek, A.M.; Capetanaki, Y.; Hwang, W.; Officer, T.; Badshah, M.; Rodarte, J.; Tidball, J.G. Desmin integrates the three-dimensional mechanical properties of muscles. Am. J. Physiol. Cell Physiol. 2001, 280, C46–C52.
  111. Heffler, J.; Shah, P.P.; Robison, P.; Phyo, S.; Veliz, K.; Uchida, K.; Bogush, A.; Rhoades, J.; Jain, R.; Prosser, B.L. A Balance between intermediate filaments and microtubules maintains nuclear architecture in the cardiomyocyte. Circ. Res. 2020, 126, e10–e26.
  112. Langer, H.T.; Mossakowski, A.A.; Willis, B.J.; Grimsrud, K.N.; Wood, J.A.; Lloyd, K.C.K.; Zbinden-Foncea, H.; Baar, K. Generation of desminopathy in rats using CRISPR-Cas9. J. Cachexiasarcopenia Muscle 2020.
  113. Starr, D.A.; Fridolfsson, H.N. Interactions Between nuclei and the cytoskeleton are mediated by SUN-KASH Nuclear-envelope bridges. Annu. Rev. Cell Dev. Biol. 2010, 26, 421–444.
  114. Lombardi, M.L.; Lammerding, J. Keeping the LINC: The importance of nucleocytoskeletal coupling in intracellular force transmission and cellular function. Biochem. Soc. Trans. 2011, 39, 1729–1734.
  115. Torbati, M.; Lele, T.P.; Agrawal, A. An unresolved LINC in the nuclear envelope. Cell. Mol. Bioeng. 2016, 9, 252–257.
  116. Zhang, Q.; Skepper, J.N.; Yang, F.; Davies, J.D.; Hegyi, L.; Roberts, R.G.; Weissberg, P.L.; Ellis, J.A.; Shanahan, C.M. Nesprins: A novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues. J. Cell Sci. 2001, 114, 4485–4498.
  117. Roux, K.J.; Crisp, M.L.; Liu, Q.; Kim, D.; Kozlov, S.; Stewart, C.L.; Burke, B. Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization. Proc. Natl. Acad. Sci. USA 2009, 106, 2194–2199.
  118. Randles, K.N.; Lam, L.T.; Sewry, C.A.; Puckelwartz, M.; Furling, D.; Wehnert, M.; McNally, E.M.; Morris, G.E. Nesprins, but not sun proteins, switch isoforms at the nuclear envelope during muscle development. Dev. Dyn. 2010, 239, 998–1009.
  119. Holt, I.; Fuller, H.R.; Lam, L.T.; Sewry, C.A.; Shirran, S.L.; Zhang, Q.; Shanahan, C.M.; Morris, G.E. Nesprin-1-alpha2 associates with kinesin at myotube outer nuclear membranes, but is restricted to neuromuscular junction nuclei in adult muscle. Sci. Rep. 2019, 9, 14202.
  120. Wilson, M.H.; Holzbaur, E.L.F. Nesprins anchor kinesin-1 motors to the nucleus to drive nuclear distribution in muscle cells. Development 2015, 142, 218–228.
  121. Chapman, M.A.; Zhang, J.; Banerjee, I.; Guo, L.T.; Zhang, Z.; Shelton, G.D.; Ouyang, K.; Lieber, R.L.; Chen, J. Disruption of both nesprin 1 and desmin results in nuclear anchorage defects and fibrosis in skeletal muscle. Hum. Mol. Genet. 2014, 23, 5879–5892.
  122. Zhang, Q. Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle. J. Cell Sci. 2005, 118, 673–687.
  123. Tapley, E.C.; Starr, D.A. Connecting the nucleus to the cytoskeleton by SUN–KASH bridges across the nuclear envelope. Curr. Opin. Cell Biol. 2013, 25, 57–62.
  124. Rajgor, D.; Mellad, J.A.; Autore, F.; Zhang, Q.; Shanahan, C.M. Multiple novel nesprin-1 and nesprin-2 Variants act as versatile tissue-specific intracellular scaffolds. PLoS ONE 2012, 7, e40098.
  125. Puckelwartz, M.J.; Kessler, E.; Zhang, Y.; Hodzic, D.; Randles, K.N.; Morris, G.; Earley, J.U.; Hadhazy, M.; Holaska, J.M.; Mewborn, S.K.; et al. Disruption of nesprin-1 produces an Emery Dreifuss muscular dystrophy-like phenotype in mice. Hum. Mol. Genet. 2009, 18, 607–620.
  126. Zhang, X.; Xu, R.; Zhu, B.; Yang, X.; Ding, X.; Duan, S.; Xu, T.; Zhuang, Y.; Han, M. Syne-1 and Syne-2 play crucial roles in myonuclear anchorage and motor neuron innervation. Development 2007, 134, 901–908.
  127. Zhang, J.; Felder, A.; Liu, Y.; Guo, L.T.; Lange, S.; Dalton, N.D.; Gu, Y.; Peterson, K.L.; Mizisin, A.P.; Shelton, G.D.; et al. Nesprin 1 is critical for nuclear positioning and anchorage. Hum. Mol. Genet. 2010, 19, 329–341.
  128. Duong, N.T.; Morris, G.E.; Lam, L.T.; Zhang, Q.; Sewry, C.A.; Shanahan, C.M.; Holt, I. Nesprins: Tissue-specific expression of epsilon and other short isoforms. PLoS ONE 2014, 9, e94380.
  129. Mislow, J.M.K.; Holaska, J.M.; Kim, M.S.; Lee, K.K.; Segura-Totten, M.; Wilson, K.L.; McNally, E.M. Nesprin-1α self-associates and binds directly to emerin and lamin A in vitro. FEBS Lett. 2002, 525, 135–140.
  130. Wheeler, M.A.; Davies, J.D.; Zhang, Q.; Emerson, L.J.; Hunt, J.; Shanahan, C.M.; Ellis, J.A. Distinct functional domains in nesprin-1α and nesprin-2β bind directly to emerin and both interactions are disrupted in X-linked Emery–Dreifuss muscular dystrophy. Exp. Cell Res. 2007, 313, 2845–2857.
  131. Holt, I.; Duong, N.T.; Zhang, Q.; Lam, L.T.; Sewry, C.A.; Mamchaoui, K.; Shanahan, C.M.; Morris, G.E. Specific localization of nesprin-1-α2, the short isoform of nesprin-1 with a KASH domain, in developing, fetal and regenerating muscle, using a new monoclonal antibody. BMC Cell Biol. 2016, 17, 26.
  132. Roman, W.; Gomes, E.R. Nuclear positioning in skeletal muscle. Semin. Cell Dev. Biol. 2018, 82, 51–56.
  133. Zhou, C.; Rao, L.; Shanahan, C.M.; Zhang, Q. Nesprin-1/2: Roles in nuclear envelope organisation, myogenesis and muscle disease. Biochem. Soc. Trans. 2018, 46, 311–320.
  134. Liao, L.; Qu, R.; Ouang, J.; Dai, J. A glance at the nuclear envelope spectrin repeat protein 3. Biomed Res. Int. 2019, 2019, 1651805.
  135. Ketema, M.; Wilhelmsen, K.; Kuikman, I.; Janssen, H.; Hodzic, D.; Sonnenberg, A. Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin. J. Cell Sci. 2007, 120, 3384–3394.
  136. Wiche, G. Role of plectin in cytoskeleton organization and dynamics. J. Cell Sci. 1998, 111, 2477–2486.
  137. Staszewska, I.; Fischer, I.; Wiche, G. Plectin isoform 1-dependent nuclear docking of desmin networks affects myonuclear architecture and expression of mechanotransducers. Hum. Mol. Genet. 2015, 24, 7373–7389.
  138. Folker, E.S.; Östlund, C.; Luxton, G.W.G.; Worman, H.J.; Gundersen, G.G. Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement. Proc. Natl. Acad. Sci. USA 2011, 108, 131–136.
  139. Ho, C.Y.; Lammerding, J. Lamins at a glance. J. Cell Sci. 2012, 125, 2087–2093.
  140. Hieda, M. Signal Transduction across the Nuclear envelope: Role of the LINC complex in bidirectional signaling. Cells 2019, 8, 124.
  141. Burke, B.; Roux, K.J. Nuclei Take a position: Managing nuclear location. Dev. Cell 2009, 17, 587–597.
  142. Fridolfsson, H.N.; Ly, N.; Meyerzon, M.; Starr, D.A. UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope during nuclear migration. Dev. Biol. 2010, 338, 237–250.
  143. Jain, N.; Iyer, K.V.; Kumar, A.; Shivashankar, G.V. Cell geometric constraints induce modular gene-expression patterns via redistribution of HDAC3 regulated by actomyosin contractility. Proc. Natl. Acad. Sci. USA 2013, 110, 11349–11354.
  144. Lei, K.; Zhang, X.; Ding, X.; Guo, X.; Chen, M.; Zhu, B.; Xu, T.; Zhuang, Y.; Xu, R.; Han, M. SUN1 and SUN2 play critical but partially redundant roles in anchoring nuclei in skeletal muscle cells in mice. Proc. Natl. Acad. Sci. USA 2009, 106, 10207–10212.
  145. Wu, Y.K.; Umeshima, H.; Kurisu, J.; Kengaku, M. Nesprins and opposing microtubule motors generate a point force that drives directional nuclear motion in migrating neurons. Development 2018, 145, dev158782.
  146. Kengaku, M. Cytoskeletal control of nuclear migration in neurons and non-neuronal cells. Proc. Jpn. Acad. Ser. B 2018, 94, 337–349.
  147. Zhang, Q.; Bethmann, C.; Worth, N.F.; Davies, J.D.; Wasner, C.; Feuer, A.; Ragnauth, C.D.; Yi, Q.; Mellad, J.A.; Warren, D.T.; et al. Nesprin-1 and -2 are involved in the pathogenesis of Emery–Dreifuss muscular dystrophy and are critical for nuclear envelope integrity. Hum. Mol. Genet. 2007, 16, 2816–2833.
  148. Stroud, M.J.; Feng, W.; Zhang, J.; Veevers, J.; Fang, X.; Gerace, L.; Chen, J. Nesprin 1α2 is essential for mouse postnatal viability and nuclear positioning in skeletal muscle. J. Cell Biol. 2017, 216, 1915–1924.
  149. Zhou, C.; Li, C.; Zhou, B.; Sun, H.; Koullourou, V.; Holt, I.; Puckelwartz, M.J.; Warren, D.T.; Hayward, R.; Lin, Z.; et al. Novel nesprin-1 mutations associated with dilated cardiomyopathy cause nuclear envelope disruption and defects in myogenesis. Hum. Mol. Genet. 2017, 26, 2258–2276.
  150. Schwartz, C.; Fischer, M.; Mamchaoui, K.; Bigot, A.; Lok, T.; Verdier, C.; Duperray, A.; Michel, R.; Holt, I.; Voit, T.; et al. Lamins and nesprin-1 mediate inside-out mechanical coupling in muscle cell precursors through FHOD1. Sci. Rep. 2017, 7, 1253.
  151. Jahed, Z.; Mofrad, M.R. The nucleus feels the force, LINCed in or not! Curr. Opin. Cell Biol. 2019, 58, 114–119.
  152. Li, Y.; Lovett, D.; Zhang, Q.; Neelam, S.; Kuchibhotla, R.A.; Zhu, R.; Gundersen, G.G.; Lele, T.P.; Dickinson, R.B. Moving Cell boundaries drive nuclear shaping during cell spreading. Biophys. J. 2015, 109, 670–686.
  153. Szczesny, S.E.; Mauck, R.L. The Nuclear option: Evidence Implicating the cell nucleus in mechanotransduction. J. Biomech. Eng. 2017, 139, 021006.
  154. Aebi, U.; Cohn, J.; Buhle, L.; Gerace, L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature 1986, 323, 560–564.
  155. Turgay, Y.; Eibauer, M.; Goldman, A.E.; Shimi, T.; Khayat, M.; Ben-Harush, K.; Dubrovsky-Gaupp, A.; Sapra, K.T.; Goldman, R.D.; Medalia, O. The molecular architecture of lamins in somatic cells. Nature 2017, 543, 261–264.
  156. Burke, B.; Stewart, C.L. The nuclear lamins: Flexibility in function. Nat. Rev. Mol. Cell Biol. 2013, 14, 13–24.
  157. Simon, D.N.; Wilson, K.L. The nucleoskeleton as a genome-associated dynamic ‘network of networks’. Nat. Rev. Mol. Cell Biol. 2011, 12, 695–708.
  158. Korfali, N.; Wilkie, G.S.; Swanson, S.K.; Srsen, V.; de las Heras, J.; Batrakou, D.G.; Malik, P.; Zuleger, N.; Kerr, A.R.W.; Florens, L.; et al. The nuclear envelope proteome differs notably between tissues. Nucleus 2012, 3, 552–564.
  159. Hieda, M. Implications for diverse functions of the LINC Complexes based on the structure. Cells 2017, 6, 3.
  160. Kalinowski, A.; Qin, Z.; Coffey, K.; Kodali, R.; Buehler, M.J.; Lösche, M.; Dahl, K.N. Calcium causes a Conformational change in lamin A Tail domain that promotes farnesyl-mediated membrane association. Biophys. J. 2013, 104, 2246–2253.
  161. Osmanagic-Myers, S.; Dechat, T.; Foisner, R. Lamins at the crossroads of mechanosignaling. Genes Dev. 2015, 29, 225–237.
  162. Bianchi, A.; Manti, P.G.; Lucini, F.; Lanzuolo, C. Mechanotransduction, nuclear architecture and epigenetics in Emery Dreifuss Muscular dystrophy: Tous pour un, un pour tous. Nucleus 2018, 9, 321–335.
  163. Coffinier, C.; Jung, H.J.; Nobumori, C.; Chang, S.; Tu, Y.; Barnes, R.H., 2nd; Yoshinaga, Y.; de Jong, P.J.; Vergnes, L.; Reue, K.; et al. Deficiencies in lamin B1 and lamin B2 cause neurodevelopmental defects and distinct nuclear shape abnormalities in neurons. Mol. Biol. Cell 2011, 22, 4683–4693.
  164. Dahl, K.N. The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber. J. Cell Sci. 2004, 117, 4779–4786.
  165. Shimi, T.; Kittisopikul, M.; Tran, J.; Goldman, A.E.; Adam, S.A.; Zheng, Y.; Jaqaman, K.; Goldman, R.D. Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy. Mol. Biol. Cell 2015, 26, 4075–4086.
  166. Swift, J.; Ivanovska, I.L.; Buxboim, A.; Harada, T.; Dingal, P.C.D.P.; Pinter, J.; Pajerowski, J.D.; Spinler, K.R.; Shin, J.-W.; Tewari, M.; et al. Nuclear lamin-A Scales with tissue stiffness and enhances matrix-directed differentiation. Science 2013, 341, 1240104.
  167. Buxboim, A.; Irianto, J.; Swift, J.; Athirasala, A.; Shin, J.-W.; Rehfeldt, F.; Discher, D.E. Coordinated increase of nuclear tension and lamin-A with matrix stiffness outcompetes lamin-B receptor that favors soft tissue phenotypes. Mol. Biol. Cell 2017, 28, 3333–3348.
  168. Guilluy, C.; Burridge, K. Nuclear mechanotransduction: Forcing the nucleus to respond. Nucleus 2015, 6, 19–22.
  169. Guilluy, C.; Osborne, L.D.; Van Landeghem, L.; Sharek, L.; Superfine, R.; Garcia-Mata, R.; Burridge, K. Isolated nuclei adapt to force and reveal a mechanotransduction pathway in the nucleus. Nat. Cell Biol. 2014, 16, 376–381.
  170. Bera, M.; Kotamarthi, H.C.; Dutta, S.; Ray, A.; Ghosh, S.; Bhattacharyya, D.; Ainavarapu, S.R.K.; Sengupta, K. Characterization of Unfolding mechanism of human lamin A Ig Fold by single-molecule force spectroscopy—Implications in EDMD. Biochemistry 2014, 53, 7247–7258.
  171. Buxboim, A.; Swift, J.; Irianto, J.; Spinler, K.R.; Dingal, P.C.D.P.; Athirasala, A.; Kao, Y.-R.C.; Cho, S.; Harada, T.; Shin, J.-W.; et al. Matrix Elasticity regulates lamin-A,C Phosphorylation and turnover with feedback to actomyosin. Curr. Biol. 2014, 24, 1909–1917.
  172. Xia, Y.; Pfeifer, C.R.; Cho, S.; Discher, D.E.; Irianto, J. Nuclear mechanosensing. Emerg. Top. Life Sci. 2018, 2, 713–725.
  173. Makarov, A.A.; Zou, J.; Houston, D.R.; Spanos, C.; Solovyova, A.S.; Cardenal-Peralta, C.; Rappsilber, J.; Schirmer, E.C. Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity. Nat. Commun. 2019, 10, 3056.
  174. Pajerowski, J.D.; Dahl, K.N.; Zhong, F.L.; Sammak, P.J.; Discher, D.E. Physical plasticity of the nucleus in stem cell differentiation. Proc. Natl. Acad. Sci. USA 2007, 104, 15619–15624.
  175. Guelen, L.; Pagie, L.; Brasset, E.; Meuleman, W.; Faza, M.B.; Talhout, W.; Eussen, B.H.; de Klein, A.; Wessels, L.; de Laat, W.; et al. Domain organization of human chromosomes revealed by mapping of nuclear lamina interactions. Nature 2008, 453, 948–951.
  176. Miroshnikova, Y.A.; Nava, M.M.; Wickström, S.A. Emerging roles of mechanical forces in chromatin regulation. J. Cell Sci. 2017, 130, 2243–2250.
  177. Le, H.Q.; Ghatak, S.; Yeung, C.-Y.C.; Tellkamp, F.; Günschmann, C.; Dieterich, C.; Yeroslaviz, A.; Habermann, B.; Pombo, A.; Niessen, C.M.; et al. Mechanical regulation of transcription controls Polycomb-mediated gene silencing during lineage commitment. Nat. Cell Biol. 2016, 18, 864–875.
  178. Robson, M.I.; de las Heras, J.I.; Czapiewski, R.; Lê Thành, P.; Booth, D.G.; Kelly, D.A.; Webb, S.; Kerr, A.R.W.; Schirmer, E.C. Tissue-specific Gene repositioning by muscle nuclear membrane proteins enhances repression of critical developmental genes during myogenesis. Mol. Cell 2016, 62, 834–847.
  179. Donnaloja, F.; Carnevali, F.; Jacchetti, E.; Raimondi, M.T. Lamin A/C Mechanotransduction in laminopathies. Cells 2020, 9, 1306.
  180. Gruenbaum, Y.; Foisner, R. Lamins: Nuclear Intermediate filament proteins with fundamental functions in nuclear mechanics and genome regulation. Annu. Rev. Biochem. 2015, 84, 131–164.
  181. Janin, A.; Gache, V. Nesprins and Lamins in health and diseases of cardiac and skeletal muscles. Front. Physiol. 2018, 9, 1277.
  182. Brull, A.; Morales Rodriguez, B.; Bonne, G.; Muchir, A.; Bertrand, A.T. The Pathogenesis and therapies of striated muscle laminopathies. Front. Physiol. 2018, 9, 1533.
  183. Quijano-Roy, S.; Mbieleu, B.; Bönnemann, C.G.; Jeannet, P.-Y.; Colomer, J.; Clarke, N.F.; Cuisset, J.-M.; Roper, H.; De Meirleir, L.; D’Amico, A.; et al. De novo LMNA mutations cause a new form of congenital muscular dystrophy. Ann. Neurol. 2008, 64, 177–186.
  184. Lammerding, J.; Schulze, P.C.; Takahashi, T.; Kozlov, S.; Sullivan, T.; Kamm, R.D.; Stewart, C.L.; Lee, R.T. Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction. J. Clin. Investig. 2004, 113, 370–378.
  185. Lammerding, J.; Hsiao, J.; Schulze, P.C.; Kozlov, S.; Stewart, C.L.; Lee, R.T. Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells. J. Cell Biol. 2005, 170, 781–791.
  186. Hale, C.M.; Shrestha, A.L.; Khatau, S.B.; Stewart-Hutchinson, P.J.; Hernandez, L.; Stewart, C.L.; Hodzic, D.; Wirtz, D. Dysfunctional connections between the nucleus and the actin and microtubule networks in laminopathic models. Biophys. J. 2008, 95, 5462–5475.
  187. Zhang, Q.; Tamashunas, A.C.; Agrawal, A.; Torbati, M.; Katiyar, A.; Dickinson, R.B.; Lammerding, J.; Lele, T.P. Local, transient tensile stress on the nuclear membrane causes membrane rupture. Mol. Biol. Cell 2019, 30, 899–906.
  188. Earle, A.J.; Kirby, T.J.; Fedorchak, G.R.; Isermann, P.; Patel, J.; Iruvanti, S.; Moore, S.A.; Bonne, G.; Wallrath, L.L.; Lammerding, J. Mutant lamins cause nuclear envelope rupture and DNA damage in skeletal muscle cells. Nat. Mater. 2020, 19, 464–473.
  189. Solovei, I.; Wang, A.S.; Thanisch, K.; Schmidt, C.S.; Krebs, S.; Zwerger, M.; Cohen, T.V.; Devys, D.; Foisner, R.; Peichl, L.; et al. LBR and Lamin A/C sequentially tether peripheral heterochromatin and inversely regulate differentiation. Cell 2013, 152, 584–598.
  190. Mattout, A.; Pike, B.L.; Towbin, B.D.; Bank, E.M.; Gonzalez-Sandoval, A.; Stadler, M.B.; Meister, P.; Gruenbaum, Y.; Gasser, S.M. An EDMD mutation in C. elegans Lamin blocks muscle-specific gene relocation and compromises muscle integrity. Curr. Biol. 2011, 21, 1603–1614.
  191. Emerson, L.J.; Holt, M.R.; Wheeler, M.A.; Wehnert, M.; Parsons, M.; Ellis, J.A. Defects in cell spreading and ERK1/2 activation in fibroblasts with lamin A/C mutations. Biochimica et Biophysica Acta (BBA) Mol. Basis Dis. 2009, 1792, 810–821.
  192. Bertrand, A.T.; Ziaei, S.; Ehret, C.; Duchemin, H.; Mamchaoui, K.; Bigot, A.; Mayer, M.; Quijano-Roy, S.; Desguerre, I.; Lainé, J.; et al. Cellular microenvironments reveal defective mechanosensing responses and elevated YAP signaling in LMNA-mutated muscle precursors. J. Cell Sci. 2014, 127, 2873–2884.
  193. Furusawa, T.; Rochman, M.; Taher, L.; Dimitriadis, E.K.; Nagashima, K.; Anderson, S.; Bustin, M. Chromatin decompaction by the nucleosomal binding protein HMGN5 impairs nuclear sturdiness. Nat. Commun. 2015, 6, 6138.
  194. Krause, M.; Te Riet, J.; Wolf, K. Probing the compressibility of tumor cell nuclei by combined atomic force-confocal microscopy. Phys. Biol. 2013, 10, 065002.
  195. Lherbette, M.; Dos Santos, Á.; Hari-Gupta, Y.; Fili, N.; Toseland, C.P.; Schaap, I.A.T. Atomic force microscopy micro-rheology reveals large structural inhomogeneities in single cell-nuclei. Sci. Rep. 2017, 7, 8116.
  196. Schäpe, J.; Prausse, S.; Radmacher, M.; Stick, R. Influence of lamin A on the mechanical properties of amphibian oocyte nuclei measured by atomic force microscopy. Biophys. J. 2009, 96, 4319–4325.
  197. Hubner, M.R.; Spector, D.L. Chromatin dynamics. Annu Rev. Biophys. 2010, 39, 471–489.
  198. Sexton, T.; Schober, H.; Fraser, P.; Gasser, S.M. Gene regulation through nuclear organization. Nat. Struct. Mol. Biol. 2007, 14, 1049–1055.
  199. Jost, K.L.; Rottach, A.; Milden, M.; Bertulat, B.; Becker, A.; Wolf, P.; Sandoval, J.; Petazzi, P.; Huertas, D.; Esteller, M.; et al. Generation and characterization of rat and mouse monoclonal antibodies specific for MeCP2 and their use in X-inactivation studies. PLoS ONE 2011, 6, e26499.
  200. Peric-Hupkes, D.; van Steensel, B. Role of the Nuclear lamina in genome organization and gene expression. Cold Spring Harb. Symp. Quant. Biol. 2010, 75, 517–524.
  201. Schubeler, D.; Francastel, C.; Cimbora, D.M.; Reik, A.; Martin, D.I.; Groudine, M. Nuclear localization and histone acetylation: A pathway for chromatin opening and transcriptional activation of the human beta-globin locus. Genes Dev. 2000, 14, 940–950.
  202. Thomas, C.H.; Collier, J.H.; Sfeir, C.S.; Healy, K.E. Engineering gene expression and protein synthesis by modulation of nuclear shape. Proc. Natl. Acad. Sci. USA 2002, 99, 1972–1977.
  203. Heo, S.J.; Nerurkar, N.L.; Baker, B.M.; Shin, J.W.; Elliott, D.M.; Mauck, R.L. Fiber stretch and reorientation modulates mesenchymal stem cell morphology and fibrous gene expression on oriented nanofibrous microenvironments. Ann. Biomed. Eng. 2011, 39, 2780–2790.
  204. Driscoll, T.P.; Cosgrove, B.D.; Heo, S.J.; Shurden, Z.E.; Mauck, R.L. Cytoskeletal to Nuclear strain transfer regulates YAP Signaling in mesenchymal stem cells. Biophys. J. 2015, 108, 2783–2793.
  205. Banerjee, I.; Zhang, J.; Moore-Morris, T.; Pfeiffer, E.; Buchholz, K.S.; Liu, A.; Ouyang, K.; Stroud, M.J.; Gerace, L.; Evans, S.M.; et al. Targeted ablation of nesprin 1 and nesprin 2 from murine myocardium results in cardiomyopathy, altered nuclear morphology and inhibition of the biomechanical gene response. PLoS Genet. 2014, 10, e1004114.
  206. Martins, R.P.; Finan, J.D.; Guilak, F.; Lee, D.A. Mechanical regulation of nuclear structure and function. Annu. Rev. Biomed. Eng. 2012, 14, 431–455.
  207. Jakkaraju, S.; Zhe, X.; Pan, D.; Choudhury, R.; Schuger, L. TIPs are tension-responsive proteins involved in myogenic versus adipogenic differentiation. Dev. Cell 2005, 9, 39–49.
  208. Tajik, A.; Zhang, Y.; Wei, F.; Sun, J.; Jia, Q.; Zhou, W.; Singh, R.; Khanna, N.; Belmont, A.S.; Wang, N. Transcription upregulation via force-induced direct stretching of chromatin. Nat. Mater. 2016, 15, 1287–1296.
  209. Folker, E.S.; Baylies, M.K. Nuclear positioning in muscle development and disease. Front. Physiol. 2013, 4.
  210. Metzger, T.; Gache, V.; Xu, M.; Cadot, B.; Folker, E.S.; Richardson, B.E.; Gomes, E.R.; Baylies, M.K. MAP and kinesin-dependent nuclear positioning is required for skeletal muscle function. Nature 2012, 484, 120–124.
  211. Azevedo, M.; Baylies, M.K. Getting into position: Nuclear Movement in muscle cells. Trends Cell Biol. 2020, 30, 303–316.
  212. Romero, N.B. Centronuclear myopathies: A widening concept. Neuromuscul. Disord. 2010, 20, 223–228.
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