Ask about this productRelated genes to: VPS41 antibody
- Gene:
- VPS41 NIH gene
- Name:
- VPS41 subunit of HOPS complex
- Previous symbol:
- -
- Synonyms:
- HVSP41
- Chromosome:
- 7p14.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-01-31
- Date modifiied:
- 2019-01-25
Related products to: VPS41 antibody
Related articles to: VPS41 antibody
- Plasma exosomal RNA has emerged as a promising source of tumor biomarkers for early cancer detection. However, conventional expression-based markers are often limited by the need for stable reference genes. RNA editing, as a sequence-specific modification, provides internal, reference-free molecular signals, offering a potential advantage for robust and reproducible biomarker development. - Source: PubMed
Publication date: 2026/05/12
Li ZhiWu DiDeng PeiyanYang RuifengWu JianxiongPan JieqiongZou JianjunLu JiachunYang Lei - The Niemann-Pick type 1 and 2 proteins (NPC1 and NPC2) coordinate cholesterol egress from late endosomes-lysosomes (LE/LY). Proper folding, trafficking, and localization of both NPC proteins are essential for normal LE/LY cholesterol handling. Accordingly, mutations in genes cause Niemann-Pick type C (NPC) disease, a progressive neurodegenerative lysosomal cholesterol storage disorder. The routes by which NPC1 reaches the LE/LY compartment in mammalian cells are not fully elucidated. Therefore, to interrogate NPC1 trafficking, we developed genome-engineered HeLa cells expressing endogenous NPC1. We demonstrate that endogenous NPC1 localizes to the LE/LY compartment and by using protein proximity-based approaches that NPC1 resides in the same membranes as Vacuolar Protein Sorting-associated protein 41 (VPS41), one of the two unique subunits of the homotypic fusion and vacuole protein sorting complex. Loss of VPS41 increases NPC1 and Lysosomal Associated Membrane Protein 1 (LAMP1) abundance. Paradoxically, this results in marked accumulation of lysosomal cholesterol and induction of sterol regulatory element-binding protein signaling. Mechanistically, using immuno-fluorescence and electron microscopy imaging in combination with a VPS41-dependent ectopic recruitment assay, we demonstrate that this is due to a shift in the localization of NPC1 and LAMP1 from LE/LY to biosynthetic vesicles called LAMP carriers. These vesicles have been recently described to transport lysosomal-destined cargo directly from the Golgi (TGN) network to LE/LY. In conclusion, we identify NPC1 as a cargo for VPS41-dependent LAMP carriers that are instrumental for the delivery of NPC1 to LE/LY and maintaining cellular cholesterol homeostasis. - Source: PubMed
Publication date: 2025/12/26
Ndoj KlevisTantucci MatteoSanza PaoloZubak KristianMarodin GiorgiaKingma JeninaSnijder FelixVeenendaal TinekeKober Daniel LZelcer NoamKlumperman Judith - Understanding how plants regulate water loss is important for improving crop productivity. Tight control of stomatal opening and closing is essential for the uptake of CO while mitigating water vapor loss. The opening of stomata is regulated in part by homotypic vacuole fusion, which is mediated by conserved homotypic vacuole protein sorting (HOPS) and vacuolar SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptors) complexes. HOPS tethers apposing vacuole membranes and promotes the formation of trans-SNARE complexes to mediate fusion. In yeast, HOPS dissociates from the assembled SNARE complex to complete vacuole fusion, but little is known about this process in plants. HOPS-specific subunits VACUOLE PROTEIN SORTING39 (VPS39) and VPS41 are required for homotypic plant vacuole fusion, and a computational model predicted that post-translational modifications of HOPS may be needed for plant stomatal vacuole fusion. Here, we characterized a viable T-DNA insertion allele of VPS39 which demonstrated a critical role of VPS39 in stomatal vacuole fusion. We found that VPS39 has increased levels of phosphorylation at S413 when stomata are closed versus open, and that VPS39 function in stomata and embryonic development requires dynamic changes in phosphorylation. Among all HOPS and vacuolar SNARE subunits, only VPS39 showed differential levels of phosphorylation between open and closed stomata. Moreover, regions containing S413 are not conserved between plants and other organisms, suggesting plant-specific mechanisms. Our data are consistent with VPS39 phosphorylation altering vacuole dynamics in response to environmental cues, similar to well-established phosphorylation cascades that regulate ion transport during stomatal opening. - Source: PubMed
Pullen Anne-MarieBillings GrantHodgens CharlesWhite GiseleAkpa Belinda SRojas-Pierce Marcela - In metazoans, autophagosomes fuse with late endosomes (LEs)/multivesicular bodies (MVBs) to form a hybrid organelle known as an amphisome. Subsequently upon fusion with lysosomes the contents of amphisomes are degraded. While the formation of metazoan amphisomes has been well established, it has remained an open question whether amphisomes form and deliver their cargo to the central vacuole for degradation in plant cells. In this mini review, we provide an update on recent discoveries in the field of plant autophagy that demonstrate the formation of amphisome-like organelles that are generated through several distinct autophagosome/MVB fusion pathways.: CFS1: FYVE domain-containing protein; CORVET: core vacuole/endosome tethering; ER: endoplasmic reticulum; ESCRT: endosomal sorting complex required for transport; FYVE: Fab1p, YOTB, Vac1p, and EEA1; FREE1: FYVE domain protein required for endosomal sorting; HOPS: homotypic fusion and protein sorting; LEs: late endosomes; MVBs: multivesicular bodies; PtdIns3P: phosphatidylinositol-3-phosphate; SNAREs: soluble NSF attachment protein receptors; VAPVs: VPS41-associated phagic vacuoles. - Source: PubMed
Publication date: 2025/11/23
Lan Hu-JiaoHuang Min-JunBednarek Sebastian YLiu Jian-Zhong - Colorectal cancer metastasis remains a major cause of cancer-related mortality, with the Metastasis-Associated in Colon Cancer 1 (MACC1) protein emerging as a critical regulator of tumor progression. Although exosomes are recognized mediators of oncogenic communication, the interplay between MACC1 and exosome biology is yet to be fully explored. This study unveils a dual mechanism through which MACC1 coordinates exosome biogenesis and oncogenic cargo delivery to drive metastatic progression. We first established clinical relevance by Pearson's demonstrating a significant correlation between MACC1 expression and exosome concentration in colorectal tumors (r = 0.457, P < 0.05). Functional studies showed that MACC1-overexpressing HCT116 cells exhibited enhanced invasiveness and transmitted pro-metastatic signals via exosomes. These exosomes were significantly enriched in the c-Met oncoprotein (P < 0.05 vs. controls) and could induce epithelial-mesenchymal transition in recipient SW480 cells, significantly enhancing their migration and invasion capacities. Mechanistically, transcriptomic analysis identified several components of the exosome secretion machinery (YKT6, RAB22A, and VPS41) as downstream targets of MACC1. Promoter-binding assays confirmed that MACC1 directly activates the transcription of YKT6, a member of the Soluble N-ethylmaleimide-sensitive factor attachment protein receptor family. This protein is critical for multivesicular body-plasma membrane fusion. The transcriptional activation led to cytoplasmic accumulation of YKT6 (P < 0.05), driving a 2.9-fold increase in exosome secretion. Crucially, YKT6-mediated exosome hypersecretion facilitated the extracellular release of c-Met-enriched vesicles, establishing a feed-forward loop for metastatic propagation. Our findings delineate an integrated metastatic axis: MACC1 orchestrates (1) transcriptional upregulation of YKT6 to amplify exosome production, and (2) selective packaging of c-Met into exosomes that prime recipient cells for invasion. This dual regulatory mechanism highlights potential therapeutic targets for intercepting metastasis-specific exosome signaling in colorectal cancer. - Source: PubMed
Publication date: 2025/08/18
Hou ShenghuaiWang LingxiaoYang ChongLi YaopingLiu Haiyi