Structural and Functional Organization of the ESCRT-I Trafficking Complex
Open accessAbstract
The endosomal sorting complex required for transport (ESCRT) complexes are central to receptor downregulation, lysosome biogenesis, and budding of HIV. The yeast ESCRT-I complex contains the Vps23, Vps28, and Vps37 proteins, and its assembly is directed by the C-terminal steadiness box of Vps23, the N-terminal half of Vps28, and the C-terminal half of Vps37. The crystal structures of a Vps23:Vps28 core subcomplex and the Vps23:Vps28:Vps37 core were solved at 2.1 and 2.8 A resolution. Each subunit contains a structurally similar pair of helices that form the core. The N-terminal domain of Vps28 has a hydrophobic binding site on its surface that is conformationally dynamic. The C-terminal domain of Vps28 binds the ESCRT-II complex. The structure shows how ESCRT-I is assembled by a compact core from which the Vps23 UEV domain, the Vps28 C domain, and other domains project to bind their partners.
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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 [29]
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 [29]
Cites
Role of ESCRT-I in Retroviral Budding
Martin-Serrano, J., Zang, T., & Bieniasz, P. D. (2003) · Journal of Virology · doi:10.1128/jvi.77.8.4794-4804.2003 · Cited by 250 · see citing works
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Complex archaea that bridge the gap between prokaryotes and eukaryotes
Spang, A., Saw, J. H., Jørgensen, S. L., Zaremba-Niedzwiedzka, K., Martijn, J., Lind, A. E., van Eijk, R., Schleper, C., Guy, L., & Ettema, T. J. G. (2015) · Nature · doi:10.1038/nature14447 · Cited by 1,324 · see citing works
Vietri, M., Radulovic, M., & Stenmark, H. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0177-4 · Cited by 962 · see citing works
Endosomal and non-endosomal functions of ESCRT proteins
Slagsvold, T., Pattni, K., Malerød, L., & Stenmark, H. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.04.004 · Cited by 238 · see citing works
Budding of a Retrovirus: Some Assemblies Required
Rose, K. M., Hirsch, V. M., & Bouamr, F. (2020) · Viruses · doi:10.3390/v12101188 · Cited by 32 · see citing works
“The N-terminal domain of VPS28 binds to the C-terminal domain of TSG101 while the C-terminal domain of VPS28 binds the ESCRT-II complex, although the role of ESCRT-II in virus release remains debated [17,18,29,34].”
Background
- Authors
- Kostelansky, M. S., Sun, J., Lee, S., Kim, J., Ghirlando, R., Hierro, A., Emr, S. D., & Hurley, J. H.
- Affiliations
- National Institutes of Health (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Hurley, James H.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2006-04
- Volume
- 125
- Issue
- 1
- Pages
- 113-126
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2105211619
- Cited by
- 115
- References
- 1
- Citations by year
- 2026: 5 · 2025: 2 · 2024: 9 · 2023: 7 · 2022: 4 · 2021: 7 · 2020: 5 · 2019: 5 · 2018: 5 · 2017: 4 · 2016: 3 · 2015: 2 · 2014: 3 · 2013: 5 · 2012: 10
- FWCI
- 3.98
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- U.S. Department of Energy
- National Institutes of Health
- Office of Science
- National Institute of General Medical Sciences
- National Institute of Diabetes and Digestive and Kidney Diseases (Z01DK036118)
- National Center for Research Resources
- Basic Energy Sciences
- Biological and Environmental Research
- 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
- VPS28, protein complex formation, crystal structure, receptor down-regulation, lysosomal biogenesis, HIV budding, hydrophobic binding site, endosomal sorting
- MeSH terms
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Phenotype, Protein Conformation, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Sequence Alignment, Amino Acid Motifs, Protein Transport, Protein Interaction Mapping, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Endosomal Sorting Complexes Required for Transport
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