VPS29 (Internal)
- Known as:
- VPS29 (Internal)
- Catalog number:
- Y213572
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- VPS29 (Internal)
Related genes to: VPS29 (Internal)
- 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 (Internal)
(I) LightCycler 1. 0; (Internal Control can't be used for this system) ; (II) LightCycler2. 0; (III) PE5700, MJ_Opticon etc. single color systems; (IV) ABI7000, ABI7300, ABI7500, ABI7900, ABI StepO1.0ml Self-Standing Cryovial Internal Thread w/ O-Ring Seal1.2ml Cryogenic Vial,Self-Standing, Internal Thread1.2ml Self-Standing Cryovial Internal Thread w per O-Ring Seal1.2ml Self-Standing Cryovial Internal Thread w per Silicone Wa1.2ml Self-Standing Cryovial Internal Thread w per Washer Seal1.2ml Self-Standing Cryovial Internal Thread w/ O-Ring Seal1.2ml Self-Standing Cryovial Internal Thread w/ O-Ring Seal1.2ml Self-Standing Cryovial Internal Thread w/ Silicone Wa1.2ml Self-Standing Cryovial Internal Thread w/ Silicone Wa1.2ml Self-Standing Cryovial Internal Thread w/Washer Seal1.2ml Self-Standing Cryovial Internal Thread w/Washer Seal1.2ml Self-Standing Cryovial Internal Thread w_ O-Ring Seal1.2ml Self-Standing Cryovial Internal Thread w_ Silicone Wa1.5-times expansion model of ear dissection, external, middle & internal ear, 4 parts Related articles to: VPS29 (Internal)
- 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 - Retrograde transport is central to endomembrane homeostasis, yet the identity and origin of plant retrograde carriers remain unresolved. Prevailing models propose that plant vacuolar sorting receptors (VSRs) recycle either from multivesicular bodies (MVBs) to the trans-Golgi network (TGN) or from the TGN to the Golgi apparatus and/or endoplasmic reticulum (ER). However, the ultrastructural features of plant retrograde transport carriers remain largely unresolved. Here, we show that plant retrograde transport is likely mediated by a previously unrecognized class of MVB-derived spherical vesicles. Using correlative light and electron microscopy and three-dimensional electron tomography, we identify a distinct population of ~30-50 nm spherical vesicles adjacent to MVBs, including nascent vesicles budding from the MVB limiting membrane in Arabidopsis root cells. Immunogold labeling shows that these vesicles are enriched in retromer components and VSRs, suggesting that they possibly function as retrograde transport carriers. To investigate their biogenesis, we perform cryo-electron microscopy and liposome tubulation assays, showing that Arabidopsis SNX1 generates shorter membrane tubules than its mammalian counterpart, consistent with reduced membrane affinity linked to differences in the amphipathic helix. Notably, the SNX1-SNX2 heterodimer produces heterogeneous structures, including spherical vesicles, recapitulating in vivo observations. Lastly, knockdown of SNX1 or SNX2 results in vacuolar mislocalization and increased degradation of GFP-VSR2, and defects in SNX1 and VPS29 inhibit formation of spherical vesicles adjacent to MVBs, resulting in embryonic lethality before the globular stage. Together, these findings establish MVB-derived spherical vesicles as plant retrograde carriers and reveal a distinct SNX-mediated mechanism underlying their formation. - Source: PubMed
Publication date: 2026/03/24
Li YanbinTao RanZhang HaiWen XiaokangLeung Stephen King PongQi QingZheng XiaohuiGuo HaoxuanWu CongxianFu ZhifeiHuang XiaorongLau Wilson Chun YuJiang LiwenCui Yong - The yeast vacuole membrane forms ordered microdomains that facilitate microlipophagy under nutrient limitation. We previously found that this process involves the intracellular sorting of sphingolipids to the vacuole. While multiple vacuole protein pathways have been identified, corresponding mechanisms for lipid sorting remain undefined. Here, we use a range of approaches to identify how endocytic sorting and intraluminal transport of sphingolipids contribute to the formation of vacuole domains. To visualize sphingolipid trafficking, we employed the ceramide (Cer) analog BODIPY C12-ceramide (BODIPY-Cer), which is internalized by cells and stains the vacuole. We observed that cells lacking Vps29 and Vps30, proteins involved in endosomal sorting, show altered vacuole domains and accumulate BODIPY-Cer at sites proximal to the plasma membrane. Subsequent incorporation of endocytic-derived Cer into the vacuole is dependent on the Niemann-Pick type C2 protein (Npc2). Loss of Npc2 reduces domain formation and causes BODIPY-Cer to accumulate within the vacuole lumen. Both intravacuole trafficking of BODIPY-Cer and membrane phase separation were not dependent on Npc2's canonical receptor, Ncr1. Lipidomics of isolated vacuoles confirmed that Npc2 independently mediates sphingolipid sorting under microlipophagy conditions. In liposome assays, yeast Npc2-but not its human homolog-robustly transports an analog of inositol phosphorylceramide, a complex sphingolipid that is enriched in phase-separated vacuoles. We propose that the enlarged binding cavity of yeast Npc2 is specialized for the incorporation of sphingolipids into the vacuole membrane to support its phase separation. - Source: PubMed
Publication date: 2026/03/16
Kim HyesooLipp Nicolas-FrédéricJuarez-Contreras IsraelWong Adrian MBudin Itay