Cited by 172Cellular transport and secretionUbiquitin and proteasome pathwaysEnzyme Structure and Function

Molecular Architecture and Functional Model of the Complete Yeast ESCRT-I Heterotetramer

Open access
Kostelansky, Michael S., Schluter, Cayetana, Tam, Yuen Yi C., Lee, Sangho, Ghirlando, Rodolfo, Beach, Bridgette, Conibear, Elizabeth, Hurley, James H.·2007·Cell

Abstract

The endosomal sorting complex required for transport-I (ESCRT-I) complex, which is conserved from yeast to humans, directs the lysosomal degradation of ubiquitinated transmembrane proteins and the budding of the HIV virus. Yeast ESCRT-I contains four subunits, Vps23, Vps28, Vps37, and Mvb12. The crystal structure of the heterotetrameric ESCRT-I complex reveals a highly asymmetric complex of 1:1:1:1 subunit stoichiometry. The core complex is nearly 18 nm long and consists of a headpiece attached to a 13 nm stalk. The stalk is important for cargo sorting by ESCRT-I and is proposed to serve as a spacer regulating the correct disposition of cargo and other ESCRT components. Hydrodynamic constraints and crystallographic structures were used to generate a model of intact ESCRT-I in solution. The results show how ESCRT-I uses a combination of a rigid stalk and flexible tethers to interact with lipids, cargo, and other ESCRT complexes over a span of approximately 25 nm.

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Crossref · 10.1016/j.cell.2007.03.016

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4 of 4 references verified0 citation errors · 0 not checkable

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  • The ESCRT-I complex has a globular head with descending alpha helical hairpins, VPS28 top, VPS37 bottom, and a coiled-coil stalk.

    “The complex assumes the structure of a globular head that is oriented as a descending stack of alpha helical hairpins with VPS28 on the top and VPS37 on the bottom, with a protruding coiled-coil stalk [29,30,31,32].”

    From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [31]

  • The functional human ESCRT-I complex is a hetero-tetramer of VPS28, TSG101, VPS37, and MVB12.

    “the functional ESCRT-I complex in humans organizes itself as a hetero-tetramer composed of a single copy of VPS28, TSG101, VPS37, and MVB12.”

    From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [31]

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Authors
Kostelansky, M. S., Schluter, C., Tam, Y. Y. C., Lee, S., Ghirlando, R., Beach, B., Conibear, E., & Hurley, J. H.
Affiliations
  • National Institutes of Health (US)
  • University of British Columbia (CA)
Corresponding author
Hurley, James H.
Venue
Cell
Publisher
Elsevier BV
Published
2007-05
Volume
129
Issue
3
Pages
485-498
ISSN
0092-8674 (ISSN-L)
OpenAlex
W1976916223
Cited by
172
References
4
Citations by year
2026: 2 · 2025: 5 · 2024: 13 · 2023: 9 · 2022: 10 · 2021: 9 · 2020: 11 · 2019: 4 · 2018: 6 · 2017: 6 · 2016: 4 · 2015: 5 · 2014: 2 · 2013: 9 · 2012: 13
FWCI
6.76
Type
journal article
Language
en
Open access
Locations
  • Cell (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Institute of Diabetes and Digestive and Kidney Diseases (Z01DK036118)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
ESCRT-I, heterotetramer, VPS28, yeast, crystal structure, stalk, cargo sorting, lysosomal degradation, HIV budding, solution structure, lipid interactions, protein complex structure
MeSH terms
Cell Membrane, Models, Molecular, Protein Conformation, Endosomes, Saccharomyces cerevisiae, Molecular Structure, Crystallography, X-Ray, Protein Structure, Quaternary, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Multiprotein Complexes, Endosomal Sorting Complexes Required for Transport

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