Other names published for VPS41: CVT8, FET2, SVL2, VAM2, VPL20, YDR080W
VPS41 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Cellular Location
- Function/Process
- Genetic Interactions
- Mutants/Phenotypes
- Regulation of
- Regulatory Role
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
VPS41 - Cellular Location (22)
| Reference | Other Genes Addressed |
|---|---|
| Kulkarni A, et al. (2012) A tethering complex dimer catalyzes trans-SNARE complex formation in intracellular membrane fusion. Bioarchitecture 2(2):59-69 | |
| Russell MR, et al. (2012) Class E compartments form in response to ESCRT dysfunction in yeast due to hyperactivity of the Vps21 Rab GTPase. J Cell Sci 125(Pt 21):5208-20 | |
| Zucchi PC and Zick M (2011) Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis. Mol Biol Cell 22(23):4635-46 | |
| Cabrera M, et al. (2010) Phosphorylation of a membrane curvature-sensing motif switches function of the HOPS subunit Vps41 in membrane tethering. J Cell Biol 191(4):845-59 | |
| Angers CG and Merz AJ (2009) HOPS interacts with Apl5 at the vacuole membrane and is required for consumption of AP-3 transport vesicles. Mol Biol Cell 20(21):4563-74 | |
| Cabrera M, et al. (2009) Vps41 phosphorylation and the Rab Ypt7 control the targeting of the HOPS complex to endosome-vacuole fusion sites. Mol Biol Cell 20(7):1937-48 | |
| Hickey CM, et al. (2009) The Major Role of the Rab Ypt7p in Vacuole Fusion Is Supporting HOPS Membrane Association. J Biol Chem 284(24):16118-25 | |
| Wiederhold E, et al. (2009) The yeast vacuolar membrane proteome. Mol Cell Proteomics 8(2):380-92 | |
| Brett CL and Merz AJ (2008) Osmotic regulation of rab-mediated organelle docking. Curr Biol 18(14):1072-7 | |
| Takeda K, et al. (2008) The vacuolar V(1)/V(0)-ATPase is involved in the release of the HOPS subunit Vps41 from vacuoles, vacuole fragmentation and fusion. FEBS Lett 582(10):1558-63 | |
| Peplowska K, et al. (2007) The CORVET Tethering Complex Interacts with the Yeast Rab5 Homolog Vps21 and Is Involved in Endo-Lysosomal Biogenesis. Dev Cell 12(5):739-50 | |
| Collins KM, et al. (2005) Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion. EMBO J 24(10):1775-86 | |
| Lagrassa TJ and Ungermann C (2005) The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex. J Cell Biol 168(3):401-14 | |
| Brown CR, et al. (2003) The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery. J Biol Chem 278(28):25688-99 | |
| Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 | |
| Wang CW, et al. (2003) Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the tethering/docking stage. J Cell Biol 163(5):973-85 | |
| Price A, et al. (2000) Proteins needed for vesicle budding from the Golgi complex are also required for the docking step of homotypic vacuole fusion. J Cell Biol 148(6):1223-29 | |
| Price A, et al. (2000) The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein. J Cell Biol 148(6):1231-8 | |
| Seals DF, et al. (2000) A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion. Proc Natl Acad Sci U S A 97(17):9402-7 | |
| Rehling P, et al. (1999) Formation of AP-3 transport intermediates requires Vps41 function. Nat Cell Biol 1(6):346-53 | |
| Schwappach B, et al. (1998) Golgi localization and functionally important domains in the NH2 and COOH terminus of the yeast CLC putative chloride channel Gef1p. J Biol Chem 273(24):15110-8 | |
| Nakamura N, et al. (1997) Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in the yeast Saccharomyces cerevisiae. J Biol Chem 272(17):11344-9 |





