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Dermitzakis, I.;  Manthou, M.E.;  Meditskou, S.;  Miliaras, D.;  Kesidou, E.;  Boziki, M.;  Petratos, S.;  Grigoriadis, N.;  Theotokis, P. Molecular Signals Driving Myelinogenesis. Encyclopedia. Available online: https://encyclopedia.pub/entry/25790 (accessed on 14 May 2025).
Dermitzakis I,  Manthou ME,  Meditskou S,  Miliaras D,  Kesidou E,  Boziki M, et al. Molecular Signals Driving Myelinogenesis. Encyclopedia. Available at: https://encyclopedia.pub/entry/25790. Accessed May 14, 2025.
Dermitzakis, Iasonas, Maria Eleni Manthou, Soultana Meditskou, Dimosthenis Miliaras, Evangelia Kesidou, Marina Boziki, Steven Petratos, Nikolaos Grigoriadis, Paschalis Theotokis. "Molecular Signals Driving Myelinogenesis" Encyclopedia, https://encyclopedia.pub/entry/25790 (accessed May 14, 2025).
Dermitzakis, I.,  Manthou, M.E.,  Meditskou, S.,  Miliaras, D.,  Kesidou, E.,  Boziki, M.,  Petratos, S.,  Grigoriadis, N., & Theotokis, P. (2022, August 03). Molecular Signals Driving Myelinogenesis. In Encyclopedia. https://encyclopedia.pub/entry/25790
Dermitzakis, Iasonas, et al. "Molecular Signals Driving Myelinogenesis." Encyclopedia. Web. 03 August, 2022.
Molecular Signals Driving Myelinogenesis
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This entry is adapted from the peer-reviewed paper 10.3390/cimb44070222

As the regulator of all cognitive, sensory, and motor activity, the nervous system is the most complex biological system in humans. In order for myelinogenesis to happen, neural stem cells (NSCs) need to undergo specific developmental stages, with the process of oligodendrogenesis, as well as additional steps for the maintenance of these primary myelin sheaths.

oligodendrogenesis myelinogenesis myelin formation embryology CNS development

1. Introduction

As has been articulated from the experimental evidence, the inauguration of myelinogenesis necessitates the formation of OPCs from multipotent NSCs, which ultimately give rise to mature myelinating OLs through a multistep process (Figure 1) [1][2]. A vital step herein lies in OPCs’ ability to migrate toward miscellaneous sites and proliferate, based predominately on environmental stimuli. These cells become post-mitotic, exiting the cell cycle to express a substantial amount of myelin-associated proteins and differentiate into mature pre-myelinating OLs [3]. Following the proper recognition, targeting and ensheathing specific nerve fibers is the subsequent critical milestone where each pioneer process creates lamellar extensions that stretch and elaborate circumferentially around the target axon [2]. As a new membrane is generated at the leading edge of the forming myelin sheath’s inner tongue, which starts to resemble a spiral cross-sectional shape, the sheath continues to spread along the axonal length. The secured stability and maintenance of a newly-formed myelin sheath is the concluding event. 
Figure 1. Major cues of OPCs generation and differentiation during myelinogenesis in the prenatal period. In the neuroepithelium lining the neural tube, NSCs are under the influence of notochord-derived SHH, which drives the cells to become OPCs through OLIG2, SOX8/9/10 or follow neuronal fate (neuroblasts) via NGN1/2 and SOX1/2/3. BMP originated from the neural crest instructing NSCs to become astrocytes, controlled by HES1 as well. FOXJ1 is a crucial transcription factor for the ependymal trajectory. The positive and negative cues controlling OPCs differentiation are displayed in the upper right boxes. The hatched box depicts a representative area around sulcus limitans (between alar and basal plates). Dashed lines showcase naturally occurring processes, albeit not addressed in detail herein. ASCL1: Achaete-scute family bHLH transcription factor 1, BDNF: Brain-derived neurotrophic factor, BMP: Bone morphogenetic protein, CNTF: Ciliary neurotrophic factor, EGR1: Early growth response 1, EP: Ependymal cells, FOXJ1: Transcription factor forkhead box J1, GALC: Galactosylceramidase, GLI2: Glioma-associated oncogene family zinc finger 2, GPR17: G protein-coupled receptor 17, HES1: Hes family bHLH transcription factor 1, ID2: Inhibitor of DNA binding 2, ID4: Inhibitor of DNA binding 2, IGF-1: Insulin-like growth factor 1, JAG1: Jagged canonical Notch ligand 1, KLF6: Kruppel-like factor 6, MYRF: Myelin regulatory factor, NGN1: Neurogenin-1, NGN2: Neurogenin-2, NSC: Neural stem cells, NT-3: Neurotrophin 3, OL: Oligodendrocytes, OLIG1: Oligodendrocyte transcription factor 1, OLIG2: Oligodendrocyte transcription factor 2, OPC: Oligodendrocyte precursor cell, QKI: Quaking homolog, KH domain RNA binding, RG: Radial glia, SET domain bifurcated histone lysine methyltransferase 1, SETDB1: SHH: Sonic hedgehog signaling molecule, SIRT1: Sirtuin 1, SIRT2: Sirtuin 2, SOX: Sex-determining region Y-box transcription factor, SREBF2: Sterol regulatory element-binding transcription factor 2, T3: Triiodothyronine, TCF4: Transcription factor 4, ZFP191: Zinc finger protein 191.

2. Formation of OPCs

OPCs being generated from the ventral VZ are under the influence of the morphogen molecule Sonic hedgehog (SHH) secreted from the notochord, while the dorsal counterparts are SHH-independent [4][5]. SHH signalling drives NSCs into a neuronal or OLs lineage fate superseding the effect of bone morphogenetic proteins (BMPs) which favour astroglial generation (Figure 1) [6][7]. Early secretion of SHH promotes motor neuron lineage formation, while interaction in later time periods promotes OLs differentiation [8]. Interestingly, the concentration of SHH can be controlled by sulfatase 1 expression in the ventral neuroepithelium prior to OPCs specification [9], whereas fibroblast growth factor (FGF) signalling is of paramount importance for further OLs differentiation, especially in the spinal cord [10][11].
Oligodendrocyte transcription factor 2 (OLIG2) is the primary regulator of OPCs generation [12][13], and its gene expression can be potentially repressed throughout the pre to postnatal period by paired box 6 (PAX6), Brahma-related gene-1 (BRG1), Iroquois homeobox 3 (IRX3), histone deacetylase (HDAC) 1, HDAC2, Distal-less homeobox (DLX) 1 and DLX 2 [14][15][16][17][18][19][20]. On the other hand, oligodendrocyte transcription factor 1 (OLIG1) is activated in later stages of OLs development [21]. Interestingly, the Hes family bHLH transcription factor (HES1) can drive RG to an astrocytic phenotype [22], while co-occurrence of OLIG2 with neurogenin-1 or neurogenin-2 supports motor neuron production [17][23][24].
Members of the sex-determining region Y-box transcription factor (SOX) family, such as SOX1, SOX2, and SOX3, can also direct OPCs towards a neuronal fate [12], in contrast to SOX8, SOX9, and SOX10, which favour the turnover of NSCs to OPCs in an autonomous manner [13][14][15]. Additionally, transcription factor forkhead box J1 (FOXJ1) supports the retention of RGs as ependymal cells throughout ventricles. Lastly, glioma-associated oncogene family zinc finger 2 (GLI2), myelin transcription factor 1 (MYT1), NK2 homeobox 6 (NKX2-6), and chromodomain-helicase-DNA-binding protein 8 (CHD8), among others, are embryonic cues for OLs specification that vary within CNS regions indicating brain region specificity [16][17][18][19].

3. Migration

SHH presence is equally catalytic to OPCs migration [20]. Platelet-derived growth factor subunit A (PDGFA) and its cognate receptor, PDGF receptor alpha (PDGFRα), are essential positive drivers for OPCs migration [21]. In line with this, SOX5, SOX6, SOX9, and SOX10 stimulate the migration, ensuring PDGF responsiveness [22][23]. Chondroitin sulfate proteoglycan neuron-glia antigen 2 (NG2) and ephrin-B2/B3 molecules control OPCs polarity and contact abilities, promoting or intercepting migration, respectively [24][25]. Nestin, neural cell adhesion molecule (NCAM), and OLIG1 can also act as chemoattractants, determining cytoskeletal plasticity as well as OPCs motility [26][27][28][29][30]. Other migration chemoattractants are 2′,3′-cyclic nucleotide 3′ phosphodiesterase (CNPase), OLIG2, hepatocyte growth factor (HGF), thrombospondin 1, endothelin 1 (ET-1), oligodendrocyte specific protein (OSP), OSP–associated protein (OAP-1), N-cadherin (NCAD), merosin, fibronectin, and integrin subunit beta 1 (αvβ1 integrin) [31][32][33][34][35][36][37][38][39]. Spassky et al. suggested that netrin-1 is a candidate mediator for chemoattraction during migration [40]. However, other studies considered this molecule as a chemorepellent, antagonizing PDGF [41][42].
More growth factors and associated molecules, such as vascular endothelial growth factor A (VEGF-A) combined with VEFG receptor 2 (VEGFR2), can act as chemoattractant molecules for OPCs migration along with miscellaneous members of the transforming growth factor beta (TGF-β) family (e.g., BMP7 and BMP4), and Gαi-linked sphingosine-1-phosphate receptor (S1PR) 1 and S1PR3 [43][44][45]. In contrast to these specific sphingosine molecules, S1PR2 and S1PR5 negatively regulated migration [45]. Moreover, although C-X-C motif chemokine receptor (CXCR) 4, C-X-C motif chemokine ligand (CXCL) 12 and semaphorin 3F have chemoattractive effects on the OPCs migration, semaphorin 3A, CXCL1, and CXCR2 inhibit migration [40][46][47]. In addition, tenascin-c inhibited OPCs migration, whilst both claudin (CLDN) 1 and CLDN3 supported OPCs relocation, validated also in human specimens [38][48][49].

4. Proliferation

Specific driver molecules that participate in migration, such as PDGFA and PDGFRα, contribute additionally to the OPC proliferation [26][50]. Interestingly, in the spinal cord, the mitogenic effect of PDGF was enhanced by chemokine CXCL1 and CXCR2 [23][51], while CXCL12 had a proliferative effect on OPCs, mediated by its receptor CXCR4 [52]. More growth factors, such as FGF2, brain-derived neurotrophic factor (BDNF), and epidermal growth factor (EGF) are shown to play a vital role in OPCs proliferation [53][54][55].
Associate developmental pathways are also implicated in this step; PDGF-mediated proliferation depends largely on Wnt/β-catenin and PI3K/AKT/mTOR pathways [56][57]. Furthermore, jagged canonical Notch ligand 1 (JAG1) promotes OPCs proliferation and critically blocks the subsequent differentiation step [58]. Carrying on subcellular, CHD7 and CHD8 regulate gene expression in specific brain regions [59][60]. Another member of the SOX family, SOX9, supports the development of OLs in the cerebellum, regulating the timing of proliferation [61]. MYT1, NCAM, cyclin-dependent kinase inhibitor 1B (p27KIP1), oligodendrocyte myelin glycoprotein (OMgp), and tubulin polymerization promoting protein (TPPP) are negative regulator cues for OPCs proliferation [62][63][64][65][66]. Interestingly, overexpression of inhibitor of DNA binding (ID) 2 and ID4 enhances proliferation [67][68]. Similarly, expression of SHH, HGF, neurotrophin-4 (NT-4), noggin, superoxide dismutase 1 (SOD1), neurotrophin-3 (NT-3), achaete-scute family bHLH transcription factor 1 (ASCL1), PAX6, CLDN1, and CLDN3 promotes the proliferation process [20][33][49][69][70][71][72][73][74].
Integrin-mediated signalling and, more specifically, OSP, OAP-1, αvβ1 integrin, αvβ3 integrin, fibronectin and laminin are pivotal mediators in cytoskeletal remodelling of proliferating OPCs [35][75][76]. Gadea et al. revealed that ET-1 is a candidate molecule for enhancing cell migration without influencing proliferation [39]. Later, Adams and colleagues underscored that loss of ET-1 reduces OPCs proliferation in the developing SVZ via directly binding to endothelin type B receptor (ETBR) [77]. A reduced OPCs proliferation is observed in GS homeobox 1/2 (Gsx1/2) mutant embryos, whereas galectin-4 (GAL-4) treatment increased the proliferation [78][79]. At last, NRG1 and SOX2 induce cell division [80][81]; however, the latest data demonstrate that NRG1 acting via ErbB did not alter the proliferation state of OPCs [82].

5. Differentiation

OLIG1 and OLIG2 are heavily involved in the post-proliferating step of myelinogenesis, defining the initiation of OPCs differentiation (Figure 1) [30][32][83], while BMPs seem to inhibit this process by downregulating myelin protein expression [84]. The effect can be reversed by using a physiological antagonist of BMP4, such as noggin, which may restore differentiation [70][85][86]. OLIG2 appears to interact with a variety of factors, such as ASCL1, BRG1, transcription factor 4 (TCF4), and SET domain bifurcated histone lysine methyltransferase 1 (SETDB1) to ensure proper OPCs differentiation [87][88][89][90][91]. G protein-coupled receptor 17 (GPR17) can act as a downregulator of OLIG1 that negatively controls the maturation and coordinates the generation of myelinating OLs from pre-myelinating OLs through ID proteins [92]. Although overexpression of ID2 and ID4 both regulate myelin gene expression by inhibiting OLs differentiation [68][93], they are not the major in vivo repressors of differentiation [94]. Moreover, decreased levels of OLIG1 and myelin regulatory factor (MYRF) were observed under early growth response 1 (EGR1) and SOX11 overexpression, delineating the inhibitory action of the latest in OPCs differentiation [95][96]. Intriguingly, MYRF is a unique regulator participating in the late stages of OLs maturation and myelination, while the action of the other OLs’ lineage transcription factors is restricted on OPCs specification or initial differentiation of OLs [97].
SOX family proteins are also participating in the OLs differentiation. In particular, SOX2 and SOX3, through negative regulation of miR145, promote OLs maturation [98], while SOX5 and SOX6 increase PDGFRα expression, maintaining OLs in their immature state [23]. For the terminal differentiation of OLs, SOX8, SOX9, and SOX10 are required [61][99][100][101]. The state of myelinogenesis-associated gene expression is uniformly affected by NKX2-2 and NKX2-6 [19][102][103]. Ji et al. suggested a mechanism regarding NKX2-2-mediated inhibition of OLs differentiation via regulation of sirtuin 2 (SIRT2), which generally is a positive cue for OLs maturation [104]. Similarly, sirtuin 1 (SIRT1) participates in the differentiation of OPCs during development [105] through cytoskeleton-related OLs proteins. The Kruppel-like factor 6 (KLF6) is another transcription factor promoting OPCs differentiation through glycoprotein 130 (GP130)-signal transducer and transcription activator 3 (STAT3) signalling [106]. Growth factor-wise, BDNF is a regulator of OLs differentiation operating via binding to tyrosine receptor kinase B (TrkB) and enhancing the MAPK pathway to upregulate gene expression during OLs maturation [54][56][107]. Evidently, NT-3 is important for the transition of immature OLs to myelin-forming cells by recruiting c-Fos protein-activating protein kinase C (PKC) and tyrosine kinase activities [108][109]. Insulin-like growth factor 1 (IGF-1) is another main factor in assisting the development of OPCs to mature OLs [110]. In accordance with that, GRB2 associated binding protein 1 (GAB1) absence decreased OLs differentiation, acting as a novel target of PDGF [111]. Incidentally, Canoll et al. suggested that NRG1 is a negative regulator of OPCs differentiation [80], while Brinkmann et al. later demonstrated that NRG1 is required for OPCs differentiation [82].
As far as metabolism is concerned, quaking homolog, KH domain RNA binding (QKI)-5 forms a complex with sterol regulatory element-binding transcription factor 2 (SREBF2) that regulates the transcription of genes responsible for cholesterol biosynthesis in OLs during differentiation [112]. Lack of transactive response DNA-binding protein 43 (TDP-43) results in lower SREBF2 and low-density lipoprotein receptor (LDLR) expression and cholesterol levels in vitro and in vivo, indicating the potential role of TDP-43 in cholesterol homeostasis in OLs, which is linked with the proper completion of OLs development [113]. In the same manner, ectonucleotide pyrophosphatase/phosphodiesterase 6 (ENPP6) participates in OLs maturation via a supplement of OLs with choline [114]. Most importantly, triiodothyronine (T3) is a key molecule for blocking OPCs proliferation and promoting their differentiation into mature OLs [115][116]. Thyroid hormone receptor alpha (TRα) is found both in OPCs and mature OLs, whilst thyroid hormone receptor isoform beta 1 (TRβ1) is located only in mature OLs [117]. The OPCs differentiation is mediated by the TRα, while TRβ1 is responsible for promoting myelinogenesis in later stages [56]. Overexpression of HES5 decreases the levels of TRβ1 receptors, while ASCL1 increases them, demonstrating their role in regulating OLs differentiation timing [118]. The neurogenic locus notch homolog protein 1 (NOTCH1) is another receptor that also regulates the differentiation timing [119]. Interestingly, JAG1 is a receptor’s ligand responsible for inhibiting OLs differentiation, while contactin 1 (CNTN1) is another ligand with the opposite function [58][120].
Other membrane molecules which repress OPCs differentiation are NCAM and leucine-rich repeat, and Ig-like domain-containing Nogo receptor interacting protein 1 (LINGO-1) [121][122]. OLs maturation is negatively affected by GAL-4 and galactosylceramidase (GALC), while prominin-1, GLI2, p21-activated kinase 1 (PAK1), myelin-associated glycoprotein (MAG), SOD1, ciliary neurotrophic factor (CNTF), and inward rectifying potassium channel 4.1 (Kir4.1) are crucial for proper differentiation [17][74][79][123][124][125][126][127][128]. On the other hand, proper completion of OLs differentiation requires zinc finger protein 191 (ZFP191) [129]. Microtubule-associated protein 2 (MAP2), microtubule-associated protein tau (MAPT), CNPase, and TPPP may be involved in OLs differentiation by organising the microtubule system, similar to fasciculation and elongation protein zeta 1 (FEZ1), which is responsible for developing OLs processes’ arbour [66][130][131][132]. Additionally, important molecules being involved in the completion of OLs development are OMgp, brain enriched myelin-associated protein 1 (BCAS1) and glutathione (GSH) [133][134][135][136]. Myelin proteolipid protein (PLP) and myelin basic protein (MBP) are the main myelin structural proteins, but it is suggested that they play an additional role in OLs differentiation [137][138]. CLDN1 and CLDN3 control MBP, OLIG2, PLP, and SOX10 expression: these molecules are essential for OLs differentiation, indicating that claudins are needed [49]. Finally, connexin 47 (CX47) and adenosine triphosphate binding cassette subfamily D member 1 (ABCD1) may support OLs during their differentiation, aiding in gap junction coupling and reducing oxidative stress, respectively [139][140][141][142][143].

6. Ensheathment

Multiple positive cues are important for the inauguration of ensheathment (Figure 2). Amongst the prime ones with a positive effect on axon-glial junction maintenance is NCAD, which regulates the interaction between OLs processes and axons [144]. The L1 cell adhesion molecule (L1-CAM) and laminin expressed in axons bind to contactin and integrin located in OLs [145]. Upon the formation of the first loops/wraps, neurofascin 155 (NF155), located in paranodal loops, forms a well-defined complex with contactin-associated protein (CASPR) and CNTN1, transmembrane proteins which are expressed in axons [146][147][148]. The activation of this complex has a pivotal role in myelin targeting, sheath growth, organisation of paranodal loops and, therefore, supporting the axoglial junction [149][150]. However, CASPR does not participate in myelin targeting [149]. In juxtaparanodes, the axoglial junction is strengthened when transient axonal glycoprotein-1 (TAG-1), a crucial molecule for maintaining enrichment of Kv1.1/Kv1.2 channels [151], interacts with CASPR2. Regarding internodal axoglial adhesion, glial cell adhesion molecule (CADM) 4 binds to axonal CADM2 and CADM3, facilitating myelin targeting, axon wrapping, and myelin sheath growth [152]. Similarly, CADM1b strongly binds to axonal CADM2, positively regulating ensheathment and strengthening the junction [153]. In the same region of the myelin sheath, MAG binds to ganglioside in axons, especially ganglioside GD1a and GT1b, and enforces the junction’s stability [154][155].
Cimb 44 00222 g002 550
Figure 2. Axoglial driving cues for the initiation of ensheathment during myelinogenesis. A process of oligodendrocyte (blue) approaches the axon (brown) based on their surfaces’ attractive and repulsive signals. The red-colored shapes represent negative surface molecules; the green ones stand for positive and the yellow for bidirectional signals. For illustrational purposes, the paranode, juxtaparanode, and internode regions are simplified. CADM1b: Cell adhesion molecule 1b, CADM2: Cell adhesion molecule 2, CADM3: Cell adhesion molecule 3, CADM4: Cell adhesion molecule 4, CASPR: Contactin-associated protein, CASPR2: Contactin-associated protein-like 2, CNTN1: Contactin 1, EphA4: Ephrin receptor A4, EphB: Ephrin receptor B, EphB1: Ephrin receptor B1, GAL-4: Galectin-4, GD1a: Ganglioside GD1a, GT1b: Ganglioside GT1b, L1-CAM: L1 cell adhesion molecule, LINGO-1: Leucine-rich repeat and Ig-like domain-containing Nogo receptor interacting protein 1, MAG: Myelin-associated glycoprotein, NCAD: N-cadherin, NCAM: Neural cell adhesion molecule, NF155: Neurofascin 155, TAG-1: Transient axonal glycoprotein-1.
Based on several studies, ephrins (A, B) and cognate receptors (A, B) have dual roles that rely on location and expression. While ephrin receptor (Eph) A4 in OLs is activated by axonal ephrin-A1 ligand, which inhibits the stability of axoglial junctions needed for ensheathment, EphA4, expressed in the axon surface, interacts with ephrin-B, promoting myelin sheet formation [156][157]. In addition, EphB1 of axons is activated through ephrin-B in OLs, which in turn stimulates myelinogenesis [157]. The axonal ephrinB2 via binding with EphB OLs receptor influences integrin activation, reducing myelin sheet formation [157]. The list of negative cues includes LINGO-1, which is located in both axons and OLs, and self-interacts in trans to control the number of targeted axons inhibiting myelinogenesis [122][158]. The NCAM is a cell adhesion molecule negatively regulating myelinogenesis. The downregulation of this protein is essential for promoting myelin formation during development, as myelinogenesis occurs only on NCAM negative axons [159]. A somatodendritic protein, junctional adhesion molecule 2 (JAM2) inhibits oligodendroglial interaction, suppressing myelinogenesis [160]. Apart from the somatodendritic molecules, GAL-4 is expressed only to unmyelinated segments of neurons in hippocampal and cortical regions; this protein is demonstrated as the first identified inhibitor of myelinogenesis in axons [161]. Of particular interest is the possible role of OLIG1 in axonal recognition during myelinogenesis [162].

7. Myelin Sheath Growth and Preservation

The long-term membrane expansion and maintenance of the newly-formed myelin sheath is the final step in completing myelinogenesis and is utterly controlled by the major myelin proteins. The most abundant myelin proteins are PLP (>50%) and MBP (~15%), having a significant role in the stabilization of the myelin structure [2][31][163]. The disruption of PLP gene expression presents impaired membrane compaction [164]. MAG, on the other side, is the third most abundant protein in CNS myelin (~5%), and does not seem to contribute to maintenance as much as it does to the previously described initial interaction between OLs and axons [126][165]. Interestingly, myelin oligodendrocyte glycoprotein (MOG) [166][167], CNPase [31][168], myelin-associated oligodendrocyte basic protein (MOBP) [169], and OMgp [65][170][171], all minor CNS myelin proteins (<1%), need more investigation on how they influence the formation and maintenance of myelin sheaths in compact myelin.
OLs microtubule stability is mediated by MAP2 and MAPT [130], while CX32 and CX47 participate in maintenance [140]. Claudins, such as OSP, CLDN1, and CLDN3, play a pivotal role as well [49][164]. Transcription factors that participate in the lamellar extension process are SOX8, SOX10, NKX2-2, NKX6-2, and MYRF [14][101][172][173]. Transmembrane protein (TMEM) 98, which inhibits the self-cleavage of MYRF, ID4, and OLIG1, could also be involved in the process [93][174], whereas OLIG2 is expressed only until myelin membranes’ production is completed [162][175]. In addition, the ERK1/2 MAP kinase pathway is indispensable in maintaining myelinated axons via FGF–FGF receptor 1 and 2 (FGFR1 and FGFR2) [176][177]. Experiments in Hdac3-mutant optic nerves raised the possibility that HDAC3 is also necessary for myelin integrity [178].
Proper cholesterol biosynthesis is prioritized in myelinogenesis, with QKI regulating this cholesterol production via SREBF2. Specifically, QKI-5 acts synergistically with peroxisome proliferator-activated receptor beta (PPARβ)-retinoid X receptor alpha (RXRα) activating transcription of the response in fatty acid metabolism genes. This operation of QKI-5 is significant for maintaining myelin homeostasis [112]. The ceramide galactosyl transferase (CGT) is a key enzyme for catalyzing GALC synthesis, while ceramide sulfotransferase (CST) is responsible for converting GALC to sulfatide [179][180]. Both CST and CGT mutant animals showed a regionally specific loss of myelin stability [179]. Thus, GALC and sulfatide have a pivotal role in the long-term maintenance of myelin, with the GALC being more crucial for myelin development than its assembly [179][180]. Additionally, peroxisomal metabolism also influences myelin survival [181]. For example, a peroxisomal transmembrane protein responsible for very long-chain fatty metabolism is encoded by the ABCD1 gene and is key in maintaining myelin stability [143][182]. Lastly, the age-dependent changes of TMEM10 might be linked with its action in maintaining CNS myelin [183].

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Iasonas Dermitzakis
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Maria Eleni Manthou
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Dimosthenis Miliaras
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Evangelia Kesidou
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Marina Boziki
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Steven Petratos
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Nikolaos Grigoriadis
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Paschalis Theotokis
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