Other names published for VPS33: CLS14, MET27, PEP14, SLP1, VAM5, VPL25, VPT33, YLR396C
VPS33 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Other Features
- Strains/Constructs
- Techniques and Reagents
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
VPS33 - Techniques and Reagents (14)
| Reference | Other Genes Addressed |
|---|---|
| Zick M and Wickner W (2012) Phosphorylation of the effector complex HOPS by the vacuolar kinase Yck3p confers Rab nucleotide specificity for vacuole docking and fusion. Mol Biol Cell 23(17):3429-37 | |
| Kramer L and Ungermann C (2011) HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites. Mol Biol Cell 22(14):2601-11 | |
| Plemel RL, et al. (2011) Subunit organization and Rab interactions of Vps-C protein complexes that control endolysosomal membrane traffic. Mol Biol Cell 22(8):1353-63 | |
| 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 | |
| Ostrowicz CW, et al. (2010) Defined subunit arrangement and rab interactions are required for functionality of the HOPS tethering complex. Traffic 11(10):1334-46 | |
| Collins KM and Wickner WT (2007) Trans-SNARE complex assembly and yeast vacuole membrane fusion. Proc Natl Acad Sci U S A 104(21):8755-60 | |
| Fratti RA, et al. (2007) Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification. J Biol Chem 282(20):14861-7 | |
| Freimoser FM, et al. (2006) Systematic screening of polyphosphate (poly P) levels in yeast mutant cells reveals strong interdependence with primary metabolism. Genome Biol 7(11):R109 | |
| Stroupe C, et al. (2006) Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J 25(8):1579-89 | |
| Starai VJ, et al. (2005) Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae. J Biol Chem 280(17):16754-62 | |
| Wang L, et al. (2003) Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion. J Cell Biol 160(3):365-74 | |
| Laage R and Ungermann C (2001) The N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusion. Mol Biol Cell 12(11):3375-85 | |
| Vida T and Gerhardt B (1999) A cell-free assay allows reconstitution of Vps33p-dependent transport to the yeast vacuole/lysosome. J Cell Biol 146(1):85-98 | |
| Banta LM, et al. (1990) Characterization of yeast Vps33p, a protein required for vacuolar protein sorting and vacuole biogenesis. Mol Cell Biol 10(9):4638-49 | |



