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Adnan, M.; Islam, W.; Waheed, A.; Hussain, Q.; Shen, L.; Wang, J.; Liu, G. Regulatory Role of Snc1 in Endocytosis and Exocytosis. Encyclopedia. Available online: https://encyclopedia.pub/entry/45662 (accessed on 27 July 2024).
Adnan M, Islam W, Waheed A, Hussain Q, Shen L, Wang J, et al. Regulatory Role of Snc1 in Endocytosis and Exocytosis. Encyclopedia. Available at: https://encyclopedia.pub/entry/45662. Accessed July 27, 2024.
Adnan, Muhammad, Waqar Islam, Abdul Waheed, Quaid Hussain, Ling Shen, Juan Wang, Gang Liu. "Regulatory Role of Snc1 in Endocytosis and Exocytosis" Encyclopedia, https://encyclopedia.pub/entry/45662 (accessed July 27, 2024).
Adnan, M., Islam, W., Waheed, A., Hussain, Q., Shen, L., Wang, J., & Liu, G. (2023, June 15). Regulatory Role of Snc1 in Endocytosis and Exocytosis. In Encyclopedia. https://encyclopedia.pub/entry/45662
Adnan, Muhammad, et al. "Regulatory Role of Snc1 in Endocytosis and Exocytosis." Encyclopedia. Web. 15 June, 2023.
Regulatory Role of Snc1 in Endocytosis and Exocytosis
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This entry is adapted from the peer-reviewed paper 10.3390/cells12111547

Fungi are an important group of microorganisms that play crucial roles in a variety of ecological and biotechnological processes. Fungi depend on intracellular protein trafficking, which involves moving proteins from their site of synthesis to the final destination within or outside the cell. The soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) proteins are vital components of vesicle trafficking and membrane fusion, ultimately leading to the release of cargos to the target destination. The v-SNARE (vesicle-associated SNARE) Snc1 is responsible for anterograde and retrograde vesicle trafficking between the plasma membrane (PM) and Golgi. It allows for the fusion of exocytic vesicles to the PM and the subsequent recycling of Golgi-localized proteins back to the Golgi via three distinct and parallel recycling pathways. This recycling process requires several components, including a phospholipid flippase (Drs2-Cdc50), an F-box protein (Rcy1), a sorting nexin (Snx4-Atg20), a retromer submit, and the COPI coat complex. Snc1 interacts with exocytic SNAREs (Sso1/2, Sec9) and the exocytic complex to complete the process of exocytosis. It also interacts with endocytic SNAREs (Tlg1 and Tlg2) during endocytic trafficking. Snc1 has been extensively investigated in fungi and has been found to play crucial roles in various aspects of intracellular protein trafficking.

SNARE proteins protein trafficking vesicle fusion SNARE complex protein secretion Snc1

1. Introduction

Fungi are a versatile group of organisms that have widespread applications in industry, medicine, and agriculture [1]. Filamentous fungi are composed of elongated cells with multiple nuclei, enabling a complex and dynamic protein transportation system [2]. The regulation of protein transport is critical for the growth and survival of filamentous fungi, necessitating a comprehensive understanding of this mechanism. Protein synthesis initiates in the cytoplasm and the synthesized proteins are targeted to specific organelles or compartments within the cell [3]. This transportation occurs via the secretory pathway, which involves several steps. The proteins are first synthesized by ribosomes and transferred to the endoplasmic reticulum (ER). The ER carries out protein folding and modifications before being forwarded to the Golgi apparatus via transport vesicles. In the Golgi apparatus, the proteins undergo additional modifications and are finally sorted into vesicles for transport to their ultimate destinations [4]. The vesicles are transported along the cytoskeleton towards the target organelle or plasma membrane (PM) [3]. Finally, the membrane of the vesicle and that of the target membrane fuse with each other, which results in the discharge of the cargo proteins into the organelle or extracellular space [4].
Membrane fusion at the target compartment is facilitated by a group of specialized proteins known as SNAREs (Soluble N-ethylmaleimide-sensitive factor attachment protein receptors). These proteins play a critical role in ensuring the effective and coordinated fusion of the two membranes [5]. The orderly fusion of membranes requires four SNARE proteins, which form a complex via the interaction of their alpha helices. This brings the two membranes in close proximity, with the concomitant expulsion of water molecules between them. The complex formed by this trans-SNARE interaction is known as SNAREpin, while the SNARE proteins involved in this process are classified as either v-SNAREs (which are associated with the vesicle membrane) or t-SNAREs (which are associated with the target membrane) [6]. The membrane fusion is completed by recruiting an R-SNARE and a set of three Q-SNAREs, named after their specific target residues, namely arginine (R) and glutamine (Q), respectively [6][7][8]. SNARE proteins are present on a wide range of membranes, including the PM, Golgi membranes, endosomes, vacuoles, ER, and their derived vesicles [6].
Snc1 is a v-SNARE protein that plays a crucial role during the final stages of protein secretion. Specifically, it plays an indispensable role in the process of vesicle fusion with Spitzenkörper and PM [9]. The exocyst complex of yeast (Saccharomyces cerevisiae) comprises the Rab-GTPases Sec4, Rho3, and CDC42. This complex is responsible for the tethering of secretory vesicles to the PM, which is necessary for their final fusion, and this process is equally mediated by SNARE proteins [10]. The process of vesicle fusion at the PM is initiated by the formation of a binary complex between the Sso1/2 and Sec9 t-SNAREs, which later bind with Snc1 (Figure 1) [11]. Interestingly, in Trichoderma reesei, Snc1 was shown to interact with Sso2 in the apical regions, while SSO1 interacts with Snc1 in the subapical regions [9]. This localization of SNAREs at the PM suggests that there are specific routes for lateral secretion. In summary, the coordinated action of SNARE proteins, including Snc1, is essential for the regulated secretion of proteins and other molecules from cells. The specificity of the interaction between SNARE proteins and their regulators, such as the exocyst complex, provides a level of control that is essential for proper cellular function.
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Figure 1. Protein structure of Snc1 of Trichoderma reesei QM6a. (A) 3D structure of SNARE protein Snc1 (created at https://swissmodel.expasy.org (accessed on 7 April 2023)). (B) Schematic representation of Snc1 domains (created at https://smart.embl-heidelberg.de (accessed on 7 April 2023)). SNARE domain is represented in the orange color (residues 16–76) and the trans-membrane domain is represented in the dark-blue color (residues 87–109).
Generally, interactions between Snc1 and other SNARE proteins are regulated by several accessory proteins such as SM proteins (Sec1/Munc18) and Ypt1 Rab GTPase (Table 1) [12]. The “zippering” of the trans-SNARE complex brings the vesicular and target membranes in close proximity, leading to their fusion [13]. The SNARE complex then dissociates on the target membrane, aided by N-ethyl maleimide-sensitive factor (NSF) and Sec18, and enables SNARE recycling [14]. Although the mechanism of Snc1-mediated vesicle fusion in filamentous fungi is similar to that in S. cerevisiae, some notable differences exist. Filamentous fungi have a more complex cytoskeleton, which may affect vesicle transport to the cell membrane [15]. Snc1 recycling requires the involvement of Drs2-Cdc50 (a phospholipid flippase), Rcy1 (an F-box protein), Snx4-Atg20 (a sorting nexin), as well as COPI (the coat protein complex (Table 1) [16], although the exact relationship between these proteins remains unclear. Studies have shown that Snc1 is crucial for protein transport in filamentous fungi, and genetic manipulations of SNC1 result in the enhanced secretion of various enzymes such as glucose oxidase, glucoamylase, and α-amylase [17][18][19]. This research will comprehensively describe the structure and regulatory role of Snc1, its interaction with other proteins, its roles in endocytosis and exocytosis, as well as its roles in the assembly and disassembly of the SNARE complex. The impact of ubiquitination on the localization and recycling of Snc1 will also be discussed, and finally analyze some strategies for enhancing protein production through the genetic manipulation of SNC1.
Table 1. SNC1 interacting proteins of fungi.
Protein Name Function Interaction with SNC1 References
Sso1/Sso2 Vesicle fusion with plasma membrane Essential for exocytosis of secretory vesicles [20]
Sec1/Munc18 Docking of secretory vesicles and their fusion with the PM Critical for efficient vesicle fusion with plasma membrane [12]
Sec9 Docking of cargo vesicles and their fusion Fusion of the secretory vesicles and PM for efficient exocytosis [20][21]
Sec18/NSF
Sec17/SNAP		 Assembly and disassembly of SNAREs Assembly and disassembly of SNC1 mediated SNAREs [22]
Exo70/
Exo84		 Important components of exocyst complex Promotes SNC1 localization towards the exocytic sites on the PM [23][24]
Sec3 Important components of the exocyst complex Promote exocytic complex formation at the PM [23][24]
Sec5
Sec6
Sec8
Sec15
Sro7/Sro77 Exocytosis and actin organization Regulate trafficking and localization of SNC1 to specific membrane domains [25]
Cdc42 Subunit of exocyst complex Fusion of secretory vesicles and the PM [10]
Drs2-Cdc50 Phospholipid flippase (Subunit of exocyst complex) Post-endocytic recycling of SNC1 [16][26]
Rcy1 F-box protein (Subunit of exocyst complex)
Snx4-Atg20 sorting nexin (Subunit of exocyst complex)
COPI coat complex COPI coat complex surrounds the cargo vesicles for cellular transportation
ArfA Recruitment of COPI to Golgi membranes Regulate SNC1 localization and activity in the secretory pathway [27]
AP180 Functional role in endocytosis Play a cargo-specific role in SNC1 internalization [28]
Tlg1/Tlg2 t-SNAREs localized to late Golgi and endosomes Recycling of Snc1 protein from the PM towards Golgi [22]
YPT1 GTPase involved in vesicle trafficking Facilitates the fusion of vesicles [12]
Sla1 Endocytosis and actin organization SNC1 and Sla1 interaction regulates the internalization of the α-factor receptor Ste2 [29]
End3/End4 Endocytosis and actin organization Efficient endocytosis of a subset of membrane proteins [30]
Vam3/Vam7 Vesicle fusion Efficient fusion of vesicles with the vacuole [22][31]
Pep12 Endosomal and vacuolar trafficking Essential for Snc1 recycling from endosomes to PM [26][32]
Vps41 Key regulator of SNC1/2 recycling Interacts with SNC1/2 and promotes its sorting into recycling vesicles [33]
Ede1 Endocytic proteins Mediate vesicle fusion during endocytosis [34][35]
Syp1
Pal1
Vti1 Trans-Golgi network to endosome transportation of vesicles Fusion of secretory vesicles and the PM [26][32]
Sec22 ER-to-Golgi vesicular transport Can complement SNC1 in vivo [36][37]
Nyv1 Fusion of vesicles with the vacuole Efficient vesicle fusion with the vacuole [22][32]
Syn8 Endosomal t-SNARE involved in vesicle fusion Exhibits promiscuous interactions with Snc1/2 [32]
Sed5 t-SNAREs of cis-Golgi Mediate fusion of initial PM derived vesicles [38]
RSP5 Ubiquitin ligase Efficient recycling of SNC1 [30]
Rab1 Rab-GTPase Regulate vesicular trafficking Rab1 inactivation blocks SNC1 recycling from Golgi to PM [39]
Rab7 Rab-GTPase Regulate vesicular trafficking Regulate SNC1 trafficking from trans-Golgi network to PM and vice versa [40]
Ras2 Ras protein required to activate adenylate cyclase pathway Ras2-SNC1 interaction suggest a role in response to nutrient availability [41]

2. Structure of Snc1 Protein

The SNARE gene SNC1 of Fusarium graminearum encodes a protein of 118 amino acids [42]. The Trichoderma reesei SNC1-encoded protein consists of 111 amino acids and has a predicted molecular mass of approximately 13 kDa [41]. Valkonen (2003) discovered that the Snc1 protein in T. reesei shares similar identity levels of 53% and 61% with the Snc1 and Snc2 proteins of S. cerevisiae, respectively [43]. This suggests that the Snc1 of T. reesei and S. cerevisiae may have functional similarities. Likewise, the v-SNARE paralogs Snc1 and Snc2 share a 79% identical amino acid sequence and are considered to be functionally redundant in S. cerevisiae [44][45]. Therefore, the SNC genes that encode Snc proteins in S. cerevisiae are thought to be duplicated. Furthermore, in T. reesei, the arginine at position 48 of the Snc1 protein is conserved among various R-SNAREs [43]. The synaptobrevin signature sequence is the most conserved area among these proteins. It is predicted that the putative cytoplasmic helix plays an important role during SNARE complex formation in yeast [46]. The PSIPRED server predicts that SNC1 will form two α-helices during the formation of the SNARE complex [47].
Snc1 is a protein that is highly conserved in filamentous fungi, and plays a crucial role in the maintenance of cellular homeostasis by regulating various processes such as vesicular transport, endocytosis, and exocytosis [16][19][48].

3. Exocytosis

The fusion of transport vesicles (containing exocytic cargo) with PM is tightly regulated through exocytosis. The central machineries that control the operation of exocytosis include the Rab family of GTPases, SM proteins (Sec1/Munc18) and the exocytic SNARE complex [21][49]. SM proteins regulate SNARE-mediated membrane fusion [49][50]. The exocytic complex is involved in the last steps of protein secretion, specifically the fusion of late secretory vesicles with the PM. The octameric exocyst complex arbitrates the tethering of secretory vesicles, which is followed by membrane fusion enabled by the assembly and disassembly of the SNARE complex [51]. In S. cerevisiae, the exocyst complex consists of the Exo70, Exo84, Sec3, Sec5, Sec6, Sec8, and Sec15 proteins [23][24]. Furthermore, Sro7 and Sro77 are two homolog proteins involved in polarized exocytosis in yeast. They interact with Snc1 to regulate its trafficking and localization to specific membrane domains [25]. Upon the arrival of secretory vesicles at the PM, the assembly of the SNARE complex is initiated, which comprises Snc1/2 (v-SNAREs localized at the secretory vesicles), and Sso1/2 and Sec9 (t-SNAREs localized at the PM) (Figure 2) [21][50]. Snc1/2 and Sso1/2 contribute one helix each, while Sec9 offers two helices for SNARE complex formation [20][21]. Some in vitro studies have revealed that a hetero-oligomeric complex of Sec9 and Sso1 binds Snc1, but not the individual t-SNARE proteins [51]. Initially, vesicles are tethered to the exocyst sites, followed by SNARE assembly, which enables the “zipping” of the membranes and subsequent vesicle fusion, leading to exocytosis [51].
Cells 12 01547 g002 550
Figure 2. Trans-SNARE complex of the Snc1, Q-SNAREs, Rab-GTPase and SM proteins. The R-SNARE SNC1 forms a trans-SNARE complex with three Q-SNAREs (Sso1, Sso2 and Sec9). The Rab-GTPases and SM proteins (Sec1/Munc18) mediate the SNARE complex formation, as well as the docking and delivery of secretory vesicles to the plasma membrane in collaboration with SNARE proteins.
Previous research endeavors have shown that Snc1 plays an essential role in establishing polarized growth and maintaining cell wall integrity in filamentous fungi by facilitating the exocytosis of cargo-containing vesicles towards hyphal tips [48]. Thus, Snc1 is essential for promoting hyphal growth and development in these organisms [19][52]. This has been suggested by Kubicek and colleagues in T. reesei, as they found that Sso1 and Sso2 both interact with Snc1 in the subapical and apical regions of the fungal hyphae, respectively [20]. Additionally, Snc1 regulates AmyB (α-amylase) localization at the septa and hyphal tips in Fusarium odoratissimum [19]. More so, Snc1 is considered crucial for the secretion of the various hydrolytic enzymes involved in nutrient acquisition and the degradation of extracellular substrates, as well as cell wall remodeling enzymes that are necessary for cell wall biosynthesis and maintenance, underscoring its role in the growth and development of fungi [16][18][53].

4. Endocytosis

Snc1 is a well-studied endocytic cargo protein that mediates the fusion of exocytic vesicles with the PM. In S. cerevisiae, Snc1 is recycled or internalized at the polarization sites via endocytosis [54]. The protein is incorporated into the endocytic vesicle at the initial stages of endocytosis following interaction with some endocytic proteins, such as Ede1, Syp1, Sla2, and Pal1 [34][35]. Wrasman provided valuable information regarding cargo selection, early coat protein interactions, the nucleation of the Arp2/3 complex, as well as the identification of some novel proteins participating in endocytosis [35]. Another study by Shanks et al. (2012) identified Vps41 as a critical regulator of Snc1/2 recycling. They found that Vps41 interacts with Snc1/2 to promote their sorting into recycling vesicles [33].
After the delivery of vesicles-transported cargos to the PM, the rapid internalization of SNC1 occurs and it is immediately recycled back to the endosome and Golgi membranes for another round of the trafficking event [55]. Burston et al. systematically defined the genes required for Snc1 internalization using a quantitative genome-wide screening that monitors the localization of the yeast vesicle-associated membrane protein (VAMP)/synaptobrevin, a homolog of Snc1. They placed these genes into functional modules containing known and novel endocytic regulators through genetic interaction mapping, and cargo selectivity was evaluated using an array-based comparative analysis. They demonstrated that clathrin and the yeast AP180 clathrin adaptor proteins have a cargo-specific role in Snc1 internalization [28]. Snc1 interacts with the endocytic protein Sla1 to regulate the internalization of the α-factor receptor Ste2p [29]. Meanwhile, a mutation in the sorting signal based on methionine, which is in the cytoplasmic domain of Snc1, reduces endocytosis and inhibits Snc1 recycling to Golgi from PM [36]. This mutation (Snc1-M43A) also leads to reduced growth and protein secretion in yeast, the aggregation of post-Golgi secretory vesicles, and the fragmentation of vacuoles [36]. Interestingly, cells lacking the SNC1 gene exhibit deficiencies in the uptake of proteins from the cell surface during endocytosis [16]. The deletion of SNC1 in S. cerevisiae results in a blockade in the delivery of FM4-64 to the vacuole and the endocytosis of the α-factor receptor Ste2p [56]. Xu and colleagues also found that the deletion of SNC1 in S. cerevisiae results in a buildup of post-Golgi vesicles and causes secretion deficiencies [57]. Inhibitors can reduce Snc1-mediated protein secretion and alter its cellular localization. Snc1 normally localizes to the PM at the early bud stage in actively growing cells of budding yeast; however, it becomes accumulated at the Golgi after treatment with turbimycin [58]. The Snc1 ortholog in A. nidulans, SynA, is also a substrate for the sub-apical collar of endocytosis [59][60][61]. In A. oryzae, the Snc1 ortholog is predominantly observed in the Spitzenkörper, but gathers at the PM in Aoend4 mutants, signifying defective endocytosis [62]. To sum it up, these studies demonstrate that Snc1 protein plays a major role in both anterograde and retrograde protein transport between the PM and Golgi.
SNARE complex formation is highly specific, ensuring that all components are transported to their appropriate locations through the secretory pathway and then recycled back to their respective membranes for reuse. Overall, Snc1 is essential in regulating protein secretion, maintaining cell wall integrity, managing endocytosis, and responding to nutrient availability. Its significance in these cellular processes emphasizes its central role in fungal physiology. However, the exact mechanisms through which Snc1 governs these processes are still not entirely clear.

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Subjects: Cell Biology
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register :
Muhammad Adnan
,
Waqar Islam
,
Abdul Waheed
,
Quaid Hussain
,
Ling Shen
,
Juan Wang
,
Gang Liu
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Update Date: 16 Jun 2023
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