8cuk

Structural highlights

Function

PEP5_YEAST Required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. Mediates transport at the vacuolar membrane where it may be responsible for tethering transport vesicles on the target membranes. It is required for gluconeogenic growth of yeast. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion (PubMed:3062374, PubMed:10978279, PubMed:10944212, PubMed:16601699). Acts as component of the CORVET complex that is required for transport between endosome and vacuole. CORVET is an effector for the endosomal Rab GTPase VPS21 (PubMed:17488625). Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation (PubMed:22570702).^{[1] [2] [3] [4] [5] [6]}

References

1. ↑ Seals DF, Eitzen G, Margolis N, Wickner WT, Price A. A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9402-7. doi:, 10.1073/pnas.97.17.9402. PMID:10944212 doi:http://dx.doi.org/10.1073/pnas.97.17.9402
2. ↑ Srivastava A, Woolford CA, Jones EW. Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae. Genetics. 2000 Sep;156(1):105-22. PMID:10978279
3. ↑ Stroupe C, Collins KM, Fratti RA, Wickner W. Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J. 2006 Apr 19;25(8):1579-89. Epub 2006 Apr 6. PMID:16601699 doi:http://dx.doi.org/7601051
4. ↑ Peplowska K, Markgraf DF, Ostrowicz CW, Bange G, Ungermann C. The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis. Dev Cell. 2007 May;12(5):739-50. doi: 10.1016/j.devcel.2007.03.006. PMID:17488625 doi:http://dx.doi.org/10.1016/j.devcel.2007.03.006
5. ↑ Singh RK, Gonzalez M, Kabbaj MH, Gunjan A. Novel E3 ubiquitin ligases that regulate histone protein levels in the budding yeast Saccharomyces cerevisiae. PLoS One. 2012;7(5):e36295. doi: 10.1371/journal.pone.0036295. Epub 2012 May 3. PMID:22570702 doi:http://dx.doi.org/10.1371/journal.pone.0036295
6. ↑ Robinson JS, Klionsky DJ, Banta LM, Emr SD. Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol Cell Biol. 1988 Nov;8(11):4936-48. PMID:3062374