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VPS27  -  ESCRT-0 subunit protein VPS27

Saccharomyces cerevisiae S288c

Synonyms: DID7, GRD11, Golgi retention defective protein 11, N2038, SSV17, ...
 
 
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Disease relevance of VPS27

  • A peptide sequence in this domain, PTVP, is involved in the function of Vps27 in the MVB pathway, the efficient endosomal recruitment of ESCRT-I, and is related to a motif in HIV-1 Gag protein that is capable of interacting with Tsg101, the mammalian homologue of Vps23 [1].
 

High impact information on VPS27

 

Biological context of VPS27

 

Anatomical context of VPS27

  • A particularly striking pattern was observed in class E mutants (e.g., vps27) where 500-700 nm organelles (presumptive prevacuolar compartments) were intensely stained with FM 4-64 while the vacuole membrane was weakly fluorescent [11].
  • Likewise, Ste3p that had accumulated in the class E compartment en route to the vacuole could progress to the vacuole upon restoration of Vps27p function indicating that the class E compartment can act as a functional intermediate [12].
  • Upon restoration of Vps27p function, the Vps10p that had accumulated in the class E compartment could return to the Golgi apparatus and restore correct sorting of CPY [12].
  • On the other hand, traffic to the early recycling endosome is less dependent on Rab5 homologs and does not require Vps27p [13].
  • We describe a complex of Vps27p and Hse1p that localizes to endosomal compartments and is required for the recycling of Golgi proteins, formation of lumenal membranes and sorting of ubiquitinated proteins into those membranes [5].
 

Associations of VPS27 with chemical compounds

  • Of the class E Vps proteins, both the ESCRT-I complex (composed of the class E proteins Vps23, 28, and 37) and Vps27 (mammalian hepatocyte receptor tyrosine kinase substrate, Hrs) have been shown to interact with ubiquitin, a signal for entry into the MVB pathway [1].
 

Physical interactions of VPS27

  • Vps27 also bound Vps23 directly via two PSDP motifs present within the Vps27 COOH terminus [8].
 

Other interactions of VPS27

  • In a yeast mutant that accumulates an exaggerated form of the prevacuolar compartment (vps27), Grd19p was observed to localize to this compartment [14].
  • In this study we demonstrate that, whereas VPS45 and VPS27 are required for the vacuolar delivery of several membrane proteins, the vacuolar membrane protein alkaline phosphatase (ALP) reaches its final destination without the function of these two genes [15].
  • The GFP-Ysl2p staining is sensitive to a mutation in VPS27 resulting in the formation of an aberrant class E compartment, but it is not affected by a sec7 mutation [16].
  • MVP1 encodes a 59-kDa hydrophilic protein, Mvp1p, which appears to colocalize with Vps1p in vps1d and vps27 delta yeast cells [17].
  • In vps27 strains defective for both anterograde and retrograde transport out of the PVC, a loss of Inp53p function markedly accelerated the rate of transport of TGN residents A-ALP and Kex2p into the PVC [18].
 

Analytical, diagnostic and therapeutic context of VPS27

References

  1. Vps27 recruits ESCRT machinery to endosomes during MVB sorting. Katzmann, D.J., Stefan, C.J., Babst, M., Emr, S.D. J. Cell Biol. (2003) [Pubmed]
  2. Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p. Misra, S., Hurley, J.H. Cell (1999) [Pubmed]
  3. Protein sorting into multivesicular endosomes. Raiborg, C., Rusten, T.E., Stenmark, H. Curr. Opin. Cell Biol. (2003) [Pubmed]
  4. Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains. Burd, C.G., Emr, S.D. Mol. Cell (1998) [Pubmed]
  5. The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Bilodeau, P.S., Urbanowski, J.L., Winistorfer, S.C., Piper, R.C. Nat. Cell Biol. (2002) [Pubmed]
  6. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Shih, S.C., Katzmann, D.J., Schnell, J.D., Sutanto, M., Emr, S.D., Hicke, L. Nat. Cell Biol. (2002) [Pubmed]
  7. Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. Swanson, K.A., Kang, R.S., Stamenova, S.D., Hicke, L., Radhakrishnan, I. EMBO J. (2003) [Pubmed]
  8. Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome. Bilodeau, P.S., Winistorfer, S.C., Kearney, W.R., Robertson, A.D., Piper, R.C. J. Cell Biol. (2003) [Pubmed]
  9. Effects of deficiencies of STAMs and Hrs, mammalian class E Vps proteins, on receptor downregulation. Kanazawa, C., Morita, E., Yamada, M., Ishii, N., Miura, S., Asao, H., Yoshimori, T., Sugamura, K. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  10. Function of Hrs in endocytic trafficking and signalling. Raiborg, C., Bache, K.G., Mehlum, A., Stenmark, H. Biochem. Soc. Trans. (2001) [Pubmed]
  11. A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. Vida, T.A., Emr, S.D. J. Cell Biol. (1995) [Pubmed]
  12. VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae. Piper, R.C., Cooper, A.A., Yang, H., Stevens, T.H. J. Cell Biol. (1995) [Pubmed]
  13. Ordering of compartments in the yeast endocytic pathway. Prescianotto-Baschong, C., Riezman, H. Traffic (2002) [Pubmed]
  14. Retrieval of resident late-Golgi membrane proteins from the prevacuolar compartment of Saccharomyces cerevisiae is dependent on the function of Grd19p. Voos, W., Stevens, T.H. J. Cell Biol. (1998) [Pubmed]
  15. The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway. Piper, R.C., Bryant, N.J., Stevens, T.H. J. Cell Biol. (1997) [Pubmed]
  16. Yeast Ysl2p, homologous to Sec7 domain guanine nucleotide exchange factors, functions in endocytosis and maintenance of vacuole integrity and interacts with the Arf-Like small GTPase Arl1p. Jochum, A., Jackson, D., Schwarz, H., Pipkorn, R., Singer-Krüger, B. Mol. Cell. Biol. (2002) [Pubmed]
  17. The Saccharomyces cerevisiae MVP1 gene interacts with VPS1 and is required for vacuolar protein sorting. Ekena, K., Stevens, T.H. Mol. Cell. Biol. (1995) [Pubmed]
  18. A novel mechanism for localizing membrane proteins to yeast trans-Golgi network requires function of synaptojanin-like protein. Ha, S.A., Bunch, J.T., Hama, H., DeWald, D.B., Nothwehr, S.F. Mol. Biol. Cell (2001) [Pubmed]
  19. The yeast VPS5/GRD2 gene encodes a sorting nexin-1-like protein required for localizing membrane proteins to the late Golgi. Nothwehr, S.F., Hindes, A.E. J. Cell. Sci. (1997) [Pubmed]
  20. Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. Stahelin, R.V., Long, F., Diraviyam, K., Bruzik, K.S., Murray, D., Cho, W. J. Biol. Chem. (2002) [Pubmed]
 
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