VPS29 (C Terminus)
- Known as:
- VPS29 (C Terminus)
- Catalog number:
- Y213319
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- VPS29 ( Terminus)
Related genes to: VPS29 (C Terminus)
- Gene:
- VPS29 NIH gene
- Name:
- VPS29 retromer complex component
- Previous symbol:
- -
- Synonyms:
- PEP11, DC7, DC15
- Chromosome:
- 12q24.11
- Locus Type:
- gene with protein product
- Date approved:
- 2001-01-04
- Date modifiied:
- 2019-01-25
Related products to: VPS29 (C Terminus)
Related articles to: VPS29 (C Terminus)
- Atg18, Atg21 and Hsv2 are homologous proteins that fulfill macroautophagic/autophagic and non-autophagic functions. We now found that Atg21 interacts with Pep8/Vps26, Vps29 and Vps35, the components of the cargo selective complex of the retromer. We identified Atg21 residues required for retromer binding and focused on two of them. The first, T106, is part of an STS-motif, which also mediates Atg18-binding to the retromer, while in Hsv2 this motif is not conserved. As a second retromer binding residue, we identified D28 of Atg21. Interestingly, the corresponding D45 of Hsv2 also confers retromer binding, but the analogous E34 of Atg18 does not. Together, Atg18 uses binding residue 1, while Atg21 uses 1 and 2 and Hsv2 only 2. During autophagy, Atg21 organizes the Atg8-lipidation machinery by interacting with Atg16 via the bottom side of its β-propeller. Partial overlap between the Atg16 binding residues and the retromer binding residues indicates mutually exclusive interaction. Indeed, lack of Atg16 enhances Atg21 binding to the retromer. The Atg21-retromer shows vacuole fission activity, which requires both retromer binding residues and the membrane-bending activity of its loop 6 C/D. Additionally, overexpression of Atg21 led to mislocalization of the Prc1/carboxypeptidase Y cargo receptor Pep1/Vps10 from the Golgi to Vps17-positive endosomes and to Prc1 secretion. We detected a cross-talk among the different retromer complexes. In the absence of the canonical retromer component Vps5, more Atg21-retromer complexes were formed. Furthermore, the vacuole hyper-fragmentation of cells cooperatively required Atg18 and Atg21. Along this line, we found that Atg21 interacts with Atg18 and Hsv2. Atg: autophagy related, CSC: cargo specific complex (of the retromer), PAS: phagophore assembly site, Prc1/CPY/carboxypeptidase Y: proteinase C, PROPPIN: beta-propeller that binds phosphoinositides. - Source: PubMed
Publication date: 2026/05/14
Strubel NoreenFörster JanKramer FlorianThumm Michael - Mutations in several genes are known to cause familial forms of Parkinson's disease (PD), including mutations in the ( ) gene linked to late-onset, autosomal dominant PD. encodes a core subunit of the retromer complex which functions in endosomal sorting and recycling. It remains unclear how the pathogenic D620N mutation in VPS35 disrupts retromer function to induce neurodegeneration in PD. Using cell-and rodent-based models expressing D620N VPS35, we performed interactome proteomics to identify alterations underlying the pathogenic effects of D620N VPS35 in PD. Using overexpression of VPS35 variants in HEK-293T cells, we conducted tandem affinity purification (TAP) or co-immunoprecipitation (co-IP) with protein chemical crosslinking to determine the native and non-native protein interactomes of wild-type (WT) and D620N VPS35, respectively. Notably, we can confirm the reduced interaction of D620N VPS35 with components of the WASH complex. Additionally, using a viral-mediated gene transfer model of human D620N VPS35 overexpression in adult rat brain, we identify the first brain-specific protein interactome of VPS35. These overexpression models reveal remarkably similar interaction profiles of WT and D620N VPS35, suggesting that the D620N mutation has a subtle effect on the overall VPS35 protein interactome. We also conducted proteomic analysis of brain tissue from a knockin (KI) mouse model that expresses VPS35 at endogenous levels. Using co-IP from hemi-brain or striatal extracts of and KI mice, we reveal a high degree of similarity between the brain interactomes of WT and D620N VPS35, further suggesting a subtle effect of the D620N mutation on VPS35 protein interactions. Notably, in both hemi-brain and striatum, we find a selective decrease in the interaction of two known interactors, TBC1D5 and VPS29, with D620N VPS35. We also performed global proteomic analysis of striatal tissue from KI mice and reveal a high degree of similarity between WT and D620N, further suggesting a subtle effect of this mutation. Together, our study provides a comprehensive evaluation of the VPS35 protein interactome and reveals a selective effect of the PD-linked D620N mutation in mammalian cells and brain. Our study provides key insight into the mechanisms of retromer dysfunction in -linked PD. - Source: PubMed
Publication date: 2026/04/13
Williams Erin TChen XiRowlands JordanIslam Md SharifulFrye MaxwellMoore Darren J - Vacuolar protein sorting 29 (VPS29) is a pivotal component of the retromer complex, which plays a central role in endosomal trafficking. Numerous studies have investigated its functions in various eukaryotic systems; however, research in plants is still at an early stage. Moreover, the mechanisms controlling its abundance and stability remain largely unknown. In this study, we elucidated the role of constitutive photomorphogenic 1 (COP1) in regulating the abundance of Arabidopsis VPS29 (AtVPS29), a component of the trimeric retromer complex. Degradation of AtVPS29 is delayed by treatment with the proteasome inhibitor MG132, resulting in the accumulation of ubiquitinated AtVPS29 in MG132-treated plants. The AtVPS29 level is higher in mutant seedlings than in wild-type seedlings under both continuous light and dark conditions. In addition, AtVPS29 abundance is reduced in COP1-overexpressing plants compared with wild-type plants. Furthermore, COP1 directly interacts with AtVPS29, and AtVPS29 is ubiquitinated by the E3 ligase activity of COP1. Moreover, genes encoding the trimeric retromer complex components AtVPS35a and AtVPS26a are upregulated in mutants. Together, our data indicate that COP1 negatively regulates the abundance and stability of AtVPS29 through its E3 ligase activity and suggest that COP1 is involved in regulating the function of the trimeric retromer complex. - Source: PubMed
Publication date: 2026/04/11
Min Wang KiLee Seung JuSong Jong TaeSeo Hak Soo - Many proteins can reach the cell surface through a Golgi-independent unconventional protein secretion (UPS) pathway, particularly under cellular stress conditions. However, the molecular mechanisms that mediate UPS remain largely elusive. In this study, VPS26A-containing retromer complex, along with the sorting nexin SNX27, is identified as a regulator of UPS of transmembrane proteins, including the trafficking-deficient ∆F508 mutant CFTR, which causes cystic fibrosis, and the SARS-CoV-2 spike protein, associated with COVID-19. A targeted CRISPR knockout screen identified VPS26A as a key contributor in the UPS of ∆F508-CFTR. Subsequent molecular analyses revealed that SNX27 recruits ∆F508-CFTR to the VPS26A-VPS35-VPS29 retromer complex, facilitating its transport to the cell surface under UPS-inducing conditions. Additionally, VPS26A and SNX27 are necessary for UPS of the spike protein, enabling the formation of intact SARS-CoV-2 virions. These findings suggest that the retromer complex and SNX27, known for their roles in recycling endosomes, mediate previously unrecognized functions in the UPS of transmembrane proteins. - Source: PubMed
Publication date: 2026/04/06
Kim Ye JinLee ChaeyoungSeo Soo KyungRoh Jae WonLee Hye RyungHwang Su JinChang NienpingChoi Hee SeongShin Dong HoonKim Hui KwonKim Han SangCho Hyun-SooLee Jae MyunGee Heon YungLee Min GooNoh Shin Hye - The evolutionarily conserved Retromer complex, composed of Vps29, Vps26 and Vps35, is an essential regulator of endosomal retrieval of transmembrane cargo proteins. For cargo sorting and trafficking to take place, Retromer assembles into coated tubulovesicular carriers together with various sorting nexin (SNX) adaptor proteins including SNX3 and SNX27 in metazoans, and Snx3 or the dimeric Vps5-Vps17 SNX-BAR proteins in yeast. Although Retromer-coated tubulovesicular carriers are vital for its function, the in vitro reconstitution of these membrane assemblies for structural and functional studies can be technically challenging. Approaches include the use of giant unilamellar vesicles and supported membrane tubules for fluorescence imaging, or smaller multilamellar vesicles (MLVs) to generate uniform tubules for imaging by cryoelectron tomography (CryoET). This chapter describes protocols for producing MLVs for membrane binding studies of Retromer and assembling the yeast Retromer-Vps5-Vps17 heteropentameric complex for reconstituting membrane tubulation for CryoET studies. We also discuss our observations of both poorly ordered and well-ordered Retromer coats observed in this experimental setup. - Source: PubMed
Publication date: 2026/01/23
Chen Kai-EnTillu Vikas AAriotti NicholasCollins Brett M