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Gene Review

VPS28  -  vacuolar protein sorting 28 homolog (S....

Homo sapiens

Synonyms: ESCRT-I complex subunit VPS28, H-Vps28, Vacuolar protein sorting-associated protein 28 homolog
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Disease relevance of VPS28

  • Further studies of ESCRT-I revealed that TSG101 mutations that inhibited PTAP or VPS28 binding blocked HIV-1 budding [1].
  • Finally, we demonstrate that fusing EIAV Gag directly with another cellular component of the VPS machinery, VPS28, can restore efficient release of an EIAV Gag late-domain mutant [2].
  • YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42 [3].

High impact information on VPS28

  • The N-terminal domain of Vps28 has a hydrophobic binding site on its surface that is conformationally dynamic [4].
  • TSG101 and VPS28, components of the mammalian ESCRT1 (endosomal sorting complex required for transport), which is part of the cellular extravesiculation machinery critical for HIV-1 budding, are also recruited to cell surface TEMs upon virus expression, suggesting that HIV-1 egress can be gated through these newly mapped microdomains [5].
  • TSG101 and hVPS28 are localized to endosomes that contain internalized EGF receptor and label strongly for ubiquitinated proteins [6].
  • The association can also be observed between natively expressed proteins in a panel of hematopoietic and nonhematopoietic cell lines, where a second subunit of the ESCRT complex, vacuolar sorting protein 28 (Vps28), was also found to interact with Bcr [7].
  • It has been shown that ESCRT-I contains the vacuolar protein sorting (Vps) proteins Vps23, Vps28, and Vps37 [8].

Biological context of VPS28

  • Using a complementation assay in which Tsg101 is artificially recruited to sites of HIV-1 assembly, we demonstrate that the integrity of the VPS28 binding site within Tsg101 is required for particle budding [9].
  • We show through mutagenesis studies that Vps28-CTD employs its strictly conserved surface in the interaction with the ESCRT-III factor Vps20 [10].

Anatomical context of VPS28

  • In this study, we demonstrate that VPS28, a second component of ESCRT-I, binds to a sequence close to the Tsg101 C terminus and is therefore recruited to the plasma membrane by HIV-1 Gag [9].

Associations of VPS28 with chemical compounds

  • Coimmunoprecipitation and Western blotting analyses showed that VPS28, a component of the ESCRT-I complex, and Cdc42, a member of the Rho family GTP-binding proteins, interacted with the M1 protein via the YRKL motif [3].

Physical interactions of VPS28

  • We have identified the mammalian orthologue of Vps28p as a 221- amino acid cytosolic protein that interacts with TSG101/mammalian VPS23 to form part of a multiprotein complex [11].

Other interactions of VPS28

  • 2) TSG101 and VPS28 co-immunoprecipitated with VPS37B-FLAG, and the three proteins comigrated together in soluble complexes of the correct size for human ESCRT-I ( approximately 350 kDa) [1].
  • Furthermore, we present evidence that Vps28-CTD is sufficient to rescue an equine infectious anaemia virus (EIAV) Gag late domain deletion [10].

Analytical, diagnostic and therapeutic context of VPS28


  1. The human endosomal sorting complex required for transport (ESCRT-I) and its role in HIV-1 budding. Stuchell, M.D., Garrus, J.E., Müller, B., Stray, K.M., Ghaffarian, S., McKinnon, R., Kräusslich, H.G., Morham, S.G., Sundquist, W.I. J. Biol. Chem. (2004) [Pubmed]
  2. Equine infectious anemia virus utilizes host vesicular protein sorting machinery during particle release. Tanzi, G.O., Piefer, A.J., Bates, P. J. Virol. (2003) [Pubmed]
  3. YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42. Hui, E.K., Barman, S., Tang, D.H., France, B., Nayak, D.P. J. Virol. (2006) [Pubmed]
  4. Structural and functional organization of the ESCRT-I trafficking complex. Kostelansky, M.S., Sun, J., Lee, S., Kim, J., Ghirlando, R., Hierro, A., Emr, S.D., Hurley, J.H. Cell (2006) [Pubmed]
  5. Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1. Nydegger, S., Khurana, S., Krementsov, D.N., Foti, M., Thali, M. J. Cell Biol. (2006) [Pubmed]
  6. Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. Bishop, N., Horman, A., Woodman, P. J. Cell Biol. (2002) [Pubmed]
  7. Bcr interacts with components of the endosomal sorting complex required for transport-I and is required for epidermal growth factor receptor turnover. Olabisi, O.O., Mahon, G.M., Kostenko, E.V., Liu, Z., Ozer, H.L., Whitehead, I.P. Cancer Res. (2006) [Pubmed]
  8. Efficient Cargo Sorting by ESCRT-I and the Subsequent Release of ESCRT-I from Multivesicular Bodies Requires the Subunit Mvb12. Curtiss, M., Jones, C., Babst, M. Mol. Biol. Cell (2007) [Pubmed]
  9. Role of ESCRT-I in retroviral budding. Martin-Serrano, J., Zang, T., Bieniasz, P.D. J. Virol. (2003) [Pubmed]
  10. The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment. Pineda-Molina, E., Belrhali, H., Piefer, A.J., Akula, I., Bates, P., Weissenhorn, W. Traffic (2006) [Pubmed]
  11. TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes. Bishop, N., Woodman, P. J. Biol. Chem. (2001) [Pubmed]
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