Cited by 187Cellular transport and secretionAutophagy in Disease and TherapyUbiquitin and proteasome pathways

TSG101/Mammalian VPS23 and Mammalian VPS28 Interact Directly and Are Recruited to VPS4-induced Endosomes

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Bishop, Naomi, Woodman, Philip·2001·Journal of Biological Chemistry

Abstract

Class E vacuolar protein sorting (vps) proteins are required for appropriate sorting of receptors within the yeast endocytic pathway, and most probably function in the biogenesis of multivesicular bodies. 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. Co-immunoprecipitation and cross-linking experiments demonstrated that hVPS28 and TSG101 interact directly and that binding requires structural information within the conserved C-terminal portion of TSG101. TSG101 and hVPS28 are predominantly cytosolic. However, when endosomal vacuolization was induced by the expression of a dominant-negative mutant of another class E vps protein, human VPS4, a portion of both TSG101 and hVPS28 translocated to the surface of these vacuoles. We conclude that TSG101 and its interacting components are directly involved in endosomal sorting.

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Crossref · 10.1074/jbc.m009863200

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  • A triple mutant (K55D, K59D, D60A) within 54EKAYIKD60 prevented VPS28-TSG101 subcomplex from forming higher order assemblies and prevented autophagosome closure.

    “a triple mutant (K55D, K59D, and D60A, termed TM) within the 54EKAYIKD60 motif, that prevented the VPS28-TSG101 subcomplex from forming higher order assemblies in solution, which also prevented autophagosome closure [36].”

    From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [36]

  • Flower and colleagues confirmed 54EKAYIKD60 motif as critical mediator of ESCRT-I helical assembly.

    “Flower and colleagues crystallized the human ESCRT-I complex and remarkably confirmed the 54EKAYIKD60 motif as a critical mediator of ESCRT-I helical assembly.”

    From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [36]

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Authors
Bishop, N., & Woodman, P.
Affiliations
University of Manchester (GB)
Corresponding author
Woodman, Philip
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2001-04
Volume
276
Issue
15
Pages
11735-11742
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2102891026
Cited by
187
References
59
Citations by year
2025: 5 · 2024: 5 · 2023: 5 · 2022: 5 · 2021: 3 · 2020: 4 · 2019: 3 · 2018: 5 · 2017: 1 · 2016: 4 · 2015: 4 · 2014: 2 · 2013: 4 · 2012: 2
FWCI
7.91
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Research Explorer (The University of Manchester) (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords
TSG101, VPS28, VPS4, endosomal sorting, multivesicular bodies, endocytic pathway, protein-protein interaction, dominant-negative mutant, vacuolization, receptor sorting
MeSH terms
Tsg101 Protein, Adenosine Triphosphatases, Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, DNA, DNA-Binding Proteins, Fungal Proteins, Humans, Molecular Sequence Data, Precipitin Tests, Protein Binding, Endosomes, Transcription Factors, Sequence Homology, Amino Acid, Protein Structure, Secondary, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Endosomal Sorting Complexes Required for Transport

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