Genomes and Genes
Gene Symbol: VPS27
Description: ESCRT-0 subunit protein VPS27
Alias: DID7, GRD11, SSV17, VPL23, VPT27, ESCRT-0 subunit protein VPS27
Species: Saccharomyces cerevisiae S288c
- Bilodeau P, Urbanowski J, Winistorfer S, Piper R. The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nat Cell Biol. 2002;4:534-9 pubmed..These data support a model in which the Vps27p-Hse1p complex has multiple functions at the endosome, one of which is as a sorting receptor for ubiquitinated membrane proteins destined for degradation. ..
- Stringer D, Piper R. A single ubiquitin is sufficient for cargo protein entry into MVBs in the absence of ESCRT ubiquitination. J Cell Biol. 2011;192:229-42 pubmed publisher..Yet, proteins fused to a single Ub moiety were efficiently delivered to the MVB lumen, which strongly indicates that a single Ub is sufficient in sorting MVBs in the absence of ESCRT ubiquitination. ..
- Ren X, Hurley J. Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast. EMBO J. 2011;30:2130-9 pubmed publisher..structure of interacting regions of the yeast ESCRT-0 and ESCRT-I complexes reveals that PSDP motifs of the Vps27 ESCRT-0 subunit bind to a novel electropositive N-terminal site on the UEV domain of the ESCRT-I subunit Vps23 ..
- Burd C, Emr S. Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains. Mol Cell. 1998;2:157-62 pubmed..Our data establish a molecular link between Vps34 PI(3)K and several FYVE domain-containing proteins (Vac1p, Vps27p) required for vacuolar/lysosomal protein trafficking. ..
- Jensen L, Carroll M, Hall M, Harvey C, Beese S, Culotta V. Down-regulation of a manganese transporter in the face of metal toxicity. Mol Biol Cell. 2009;20:2810-9 pubmed publisher..We provide evidence that manganese starvation is sensed within the lumen of the secretory pathway, whereas manganese toxicity is sensed within an extra-Golgi/cytosolic compartment of the cell. ..
- Rue S, Mattei S, Saksena S, Emr S. Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting. Mol Biol Cell. 2008;19:475-84 pubmed..We propose a model in which the Ist1-Did2 and Vta1-Vps60 complexes independently modulate late steps in the MVB-sorting pathway. ..
- Tong Z, Kim M, Pandey A, Espenshade P. Identification of candidate substrates for the Golgi Tul1 E3 ligase using quantitative diGly proteomics in yeast. Mol Cell Proteomics. 2014;13:2871-82 pubmed publisher..This quantitative diGly proteomics methodology will serve as a robust platform for screening for stress conditions that require Tul1 E3 ligase activity. ..
- Morvan J, Rinaldi B, Friant S. Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes. Mol Biol Cell. 2012;23:4054-64 pubmed publisher..The ESCRT-0 subunit Vps27 is a key player in this pathway since it recruits the other complexes to endosomes...
- PÃ©rez Sampietro M, Herrero E. The PacC-family protein Rim101 prevents selenite toxicity in Saccharomyces cerevisiae by controlling vacuolar acidification. Fungal Genet Biol. 2014;71:76-85 pubmed publisher..In addition, a parallel Rim101-independent pathway requiring the complete ESCRT machinery (including the ESCRT-0 complex) also participates in protection against selenite. ..
- Erpapazoglou Z, Dhaoui M, Pantazopoulou M, Giordano F, Mari M, Leon S, et al. A dual role for K63-linked ubiquitin chains in multivesicular body biogenesis and cargo sorting. Mol Biol Cell. 2012;23:2170-83 pubmed publisher..A failure to generate K63Ub chains in yeast leads to an MVB ultrastructure alteration. Our work thus unravels a double function of K63Ub chains in cargo sorting and MVB biogenesis. ..
- Gabriely G, Kama R, Gerst J. Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast. Mol Cell Biol. 2007;27:526-40 pubmed..Third, we observed physical interactions and colocalization between COPIb subunits and an MVB-associated protein, Vps27. Together, our findings suggest that certain COPI subunits could have a direct role in vacuolar protein sorting to ..
- Isasa M, SuÃ±er C, DÃaz M, Puig SÃ rries P, Zuin A, Bichman A, et al. Cold Temperature Induces the Reprogramming of Proteolytic Pathways in Yeast. J Biol Chem. 2016;291:1664-75 pubmed publisher..These unanticipated observations indicate that, during cold response, there is a proteolytic cellular reprogramming in which the proteasome acquires a role in the endocytic-vacuolar pathway. ..
- Eugster A, Pécheur E, Michel F, Winsor B, Letourneur F, Friant S. Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. Mol Biol Cell. 2004;15:3031-41 pubmed..Therefore, Ent3p and Ent5p are the first proteins shown to be connectors between PtdIns(3,5)P(2)- and the Vps27p-ubiquitin-driven sorting machinery at the multivesicular body. ..
- Swaminathan S, Amerik A, Hochstrasser M. The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. Mol Biol Cell. 1999;10:2583-94 pubmed..We propose that Doa4 helps recycle ubiquitin from both proteasome-bound ubiquitinated intermediates and membrane proteins destined for destruction in the vacuole. ..
- Swanson K, Kang R, Stamenova S, Hicke L, Radhakrishnan I. Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. EMBO J. 2003;22:4597-606 pubmed..The yeast Vps27 protein requires two UIMs for efficient interactions with ubiquitin and for sorting cargo into multivesicular ..
- Peters T, Miller A, Tourette C, Agren H, Hubbard A, Hughes R. Genomic Analysis of ATP Efflux in Saccharomyces cerevisiae. G3 (Bethesda). 2015;6:161-70 pubmed publisher..These results will facilitate analysis of ATP efflux mechanisms in higher eukaryotes. ..
- Amerik A, Nowak J, Swaminathan S, Hochstrasser M. The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol Biol Cell. 2000;11:3365-80 pubmed
- Mitsui K, Koshimura Y, Yoshikawa Y, Matsushita M, Kanazawa H. The endosomal Na(+)/H(+) exchanger contributes to multivesicular body formation by regulating the recruitment of ESCRT-0 Vps27p to the endosomal membrane. J Biol Chem. 2011;286:37625-38 pubmed publisher..Taken together, we propose that Nhx1p contributes to MVB formation by the recruitment of Vps27p to the endosomal membrane, possibly through Nhx1p antiporter activity. ..
- Dieckmann A, Babin V, Harari Y, Eils R, König R, Luke B, et al. Role of the ESCRT Complexes in Telomere Biology. MBio. 2016;7: pubmed publisher..We discuss the significance of these findings and how they could be relevant to anticancer therapies. ..
- Mageswaran S, Johnson N, Odorizzi G, Babst M. Constitutively active ESCRT-II suppresses the MVB-sorting phenotype of ESCRT-0 and ESCRT-I mutants. Mol Biol Cell. 2015;26:554-68 pubmed publisher..However, the ESCRT-III/Vps4 system alone is not sufficient for ILV formation but requires cargo sorting mediated by one of the early ESCRTs. ..
- Prag G, Watson H, Kim Y, Beach B, Ghirlando R, Hummer G, et al. The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitin-dependent sorting. Dev Cell. 2007;12:973-86 pubmedThe yeast Vps27/Hse1 complex and the homologous mammalian Hrs/STAM complex deliver ubiquitinated transmembrane proteins to the ESCRT endosomal-sorting pathway...
- Manczyk N, Yates B, Veggiani G, Ernst A, Sicheri F, Sidhu S. Structural and functional characterization of a ubiquitin variant engineered for tight and specific binding to an alpha-helical ubiquitin interacting motif. Protein Sci. 2017;26:1060-1069 pubmed publisher..Here we used phage display to generate ubiquitin variants (UbVs) targeting the N-terminal UIM of the yeast Vps27 protein. Selections yielded UbV.v27...
- Valdivia R, Baggott D, Chuang J, Schekman R. The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane proteins. Dev Cell. 2002;2:283-94 pubmed..Similarly, in AP-1 deficient cells, the resident TGN/early endosome syntaxin, Tlg1p, is missorted. We propose that clathrin and AP-1 act to recycle Chs3p and Tlg1p from the early endosome to the TGN. ..
- Kucharczyk R, Hoffman Sommer M, Piekarska I, von Mollard G, Rytka J. The Saccharomyces cerevisiae protein Ccz1p interacts with components of the endosomal fusion machinery. FEMS Yeast Res. 2009;9:565-73 pubmed publisher..The genes MON1 and YPT7 also interact genetically with PEP12. These results suggest that the Ccz1p-Mon1p-Ypt7p complex is involved in fusion of transport vesicles to multiple target membranes in yeast cells. ..
- Arcones I, Sacristan C, Roncero C. Maintaining protein homeostasis: early and late endosomal dual recycling for the maintenance of intracellular pools of the plasma membrane protein Chs3. Mol Biol Cell. 2016;27:4021-4032 pubmed
- Strochlic T, Schmiedekamp B, Lee J, Katzmann D, Burd C. Opposing activities of the Snx3-retromer complex and ESCRT proteins mediate regulated cargo sorting at a common endosome. Mol Biol Cell. 2008;19:4694-706 pubmed publisher..and absence of iron, Fet3-Ftr1 transits an endosomal compartment where a subunit of the MVB sorting receptor (Vps27), Snx3/Grd19, and retromer proteins colocalize...
- Rubio Texeira M, Van Zeebroeck G, Thevelein J. Peptides induce persistent signaling from endosomes by a nutrient transceptor. Nat Chem Biol. 2012;8:400-8 pubmed publisher..Hence, this work has identified specific dipeptides that cause enhanced proton influx through the Gap1 symporter, resulting in its defective vacuolar sorting, and independently transform it into a persistently signaling transceptor. ..
- Wang S, Thibault G, Ng D. Routing misfolded proteins through the multivesicular body (MVB) pathway protects against proteotoxicity. J Biol Chem. 2011;286:29376-87 pubmed publisher..Eliminating the MVB sorting signal diverted molecules to the vacuolar limiting membrane, resulting in the generation of toxic by-products. These data demonstrate a new role of the MVB pathway in protein quality control. ..
- Libuda D, Winston F. Alterations in DNA replication and histone levels promote histone gene amplification in Saccharomyces cerevisiae. Genetics. 2010;184:985-97 pubmed publisher..Taken together, our results suggest that either reduced histone levels or slowed replication forks stimulate the HTA2-HTB2 amplification event, contributing to the restoration of normal chromatin structure. ..
- Auld K, Hitchcock A, Doherty H, Frietze S, Huang L, Silver P. The conserved ATPase Get3/Arr4 modulates the activity of membrane-associated proteins in Saccharomyces cerevisiae. Genetics. 2006;174:215-27 pubmed..In combination, our characterization of GET3 genetic and biochemical interactions with NPL4, GET1, and GET2 implicates Get3 in multiple membrane-dependent pathways. ..
- Ha S, Bunch J, Hama H, DeWald D, Nothwehr S. A novel mechanism for localizing membrane proteins to yeast trans-Golgi network requires function of synaptojanin-like protein. Mol Biol Cell. 2001;12:3175-90 pubmed..In vps27 strains defective for both anterograde and retrograde transport out of the PVC, a loss of Inp53p function markedly ..
- Luo W, Chang A. Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant. J Cell Biol. 1997;138:731-46 pubmed..Thus, cell surface delivery of mutant Pma1 can occur as a consequence of disturbances at several different sites in the endosomal system. ..
- Russell M, Shideler T, Nickerson D, West M, Odorizzi G. Class E compartments form in response to ESCRT dysfunction in yeast due to hyperactivity of the Vps21 Rab GTPase. J Cell Sci. 2012;125:5208-20 pubmed publisher..Indeed, genetic disruption of Rab conversion without ESCRT dysfunction autonomously drives the class E compartment morphology without blocking ILV budding. ..
- Bowers K, Lottridge J, Helliwell S, Goldthwaite L, Luzio J, Stevens T. Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae. Traffic. 2004;5:194-210 pubmed..We propose the formation of a large multimeric complex on the endosome membrane consisting of ESCRTI, ESCRTII, ESCRTIII and other associated proteins. ..