Antibodies: VPS41 HOST: Goat Clonality: pAb
- Known as:
- Antibodies: VPS41 HOST: Goat Clonality: pAb
- Catalog number:
- CA17942-100
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biomatic
- Gene target:
- Antibodies: VPS41 HOST: Goat Clonality: pAb
Related genes to: Antibodies: VPS41 HOST: Goat Clonality: pAb
- Gene:
- CERNA2 NIH gene
- Name:
- competing endogenous lncRNA 2 for microRNA let-7b
- Previous symbol:
- -
- Synonyms:
- HOST2
- Chromosome:
- 10q23.1
- Locus Type:
- RNA, long non-coding
- Date approved:
- 2017-04-27
- Date modifiied:
- 2017-07-14
- 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: Antibodies: VPS41 HOST: Goat Clonality: pAb
Alkaline Phosphatase Conjugated Affinity Purified anti-Swine IgG (H&L) [Goat] Secondary_Antibodies Alkaline Phosphatase Conjugated Affinity Purified anti_Swine IgG (H&L) [Goat] guanine nucleotide binding protein alpha inhibiting activity polypeptide 1 (GNAI1) polyclonal antibody kinase suppressor of ras (KSR) polyclonal antibody'F 4_80 Antigen (mouse) Host Rat'F 4_80 Antigen (mouse) Host Rat(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host Guinea Pig(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host Rabbit(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host: Guinea Pig(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host: Guinea Pig(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host: Rabbit(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host: Rabbit(Arg8)-Vasopressin - EIA Kit (H - sr, pl), Host Rabbit, Extraction-free, CE-marked(Arg8)-Vasopressin - EIA Kit (H - sr, pl), Host Rabbitî ‚Extraction-freeî ‚CE-marked(Arg8)-Vasopressin - EIA Kit (H - sr, pl), Host: Rabbit, Extraction-free, CE-marked Related articles to: Antibodies: VPS41 HOST: Goat Clonality: pAb
- Macroautophagy/autophagy serves as a crucial cellular defense mechanism against invading pathogens. However, viruses have evolved diverse strategies to evade or even exploit autophagy for their own replication. In this study, we reveal that the African swine fever virus (ASFV)-encoded I10L protein suppresses autophagy by blocking autophagosome-lysosome fusion. Mechanistically, I10L directly interacts with the endolysosomal RAB GTPase RAB7, a master regulator of vesicle docking at late endosomes and lysosomes. This interaction competitively prevents RAB7 from binding to VPS39, a core component of the homotypic fusion and vacuole protein sorting (HOPS) complex. Consequently, I10L disrupts the assembly of the STX17-SNAP29-VAMP8 SNARE complex, which is essential for autophagosome-lysosome fusion. ASFV infection thus induces autophagosome accumulation, whereas I10L deletion reverses this effect and attenuates viral replication in primary macrophages. Our findings uncover a novel immune evasion strategy by which ASFV subverts lysosomal degradation through RAB7-HOPS axis manipulation, providing both mechanistic insights into viral pathogenicity and potential therapeutic targets for antiviral development. ASFV: African swine fever virus; GEF: guanine nucleotide exchange factor; GFP: green fluorescent protein; HOPS: homotypic fusion and vacuole protein sorting; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; PAMs: primary alveolar macrophages; RAB7: RAB7, member RAS oncogene family; siRNA: small interfering RNA; SNAP29: synaptosome associated protein 29; SNARE: soluble N-ethylmaleimide-sensitive factor attachment protein receptor; SQSTM1/p62: sequestosome 1; STX17: syntaxin 17; TM: transmembrane domain; VAMP8: vesicle associated membrane protein 8; VPS39: VPS39 subunit of HOPS complex; VPS41: VPS41 subunit of HOPS complex; YKT6: YKT6 vesicular SNARE protein. - Source: PubMed
Publication date: 2026/05/15
Chen MengSunkang YongjieCheng TongLiu LeiLi HuananYuan HuajinHuang LihongSun LeiQi WenbaoShang Yingli - 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