The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structural basis for ESCRT-III protein autoinhibition
Open accessAbstract
Endosomal sorting complexes required for transport-III (ESCRT-III) subunits cycle between two states: soluble monomers and higher-order assemblies that bind and remodel membranes during endosomal vesicle formation, midbody abscission and enveloped virus budding. Here we show that the N-terminal core domains of increased sodium tolerance-1 (IST1) and charged multivesicular body protein-3 (CHMP3) form equivalent four-helix bundles, revealing that IST1 is a previously unrecognized ESCRT-III family member. IST1 and its ESCRT-III binding partner, CHMP1B, both form higher-order helical structures in vitro, and IST1-CHMP1 interactions are required for abscission. The IST1 and CHMP3 structures also reveal that equivalent downstream α5 helices can fold back against the core domains. Mutations within the CHMP3 core–α5 interface stimulate the protein's in vitro assembly and HIV-inhibition activities, indicating that dissociation of the autoinhibitory α5 helix from the core activates ESCRT-III proteins for assembly at membranes.
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Citations
Cites
Biogenesis and Function of Multivesicular Bodies
Piper, R. C., & Katzmann, D. J. (2007) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123319 · Cited by 771
Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
Hanson, P. I., Roth, R., Lin, Y., & Heuser, J. E. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200707031 · Cited by 427
Cited by
HIV-1 assembly, budding, and maturation
Sundquist, W. I., & Krausslich, H.-G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006924 · Cited by 814
Self-citationMolecular mechanism of multivesicular body biogenesis by ESCRT complexes
Wollert, T., & Hurley, J. H. (2010) · Nature · doi:10.1038/nature08849 · Cited by 804
Cytokinetic Abscission: Molecular Mechanisms and Temporal Control
Mierzwa, B., & Gerlich, D. W. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.11.006 · Cited by 288
ESCRT-III protein requirements for HIV-1 budding
Morita, E., Sandrin, V., McCullough, J., Katsuyama, A., Baci Hamilton, I., & Sundquist, W. I. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.02.004 · Cited by 242
Self-citationALIX and ESCRT-I/II function as parallel ESCRT-III recruiters in cytokinetic abscission
Christ, L., Wenzel, E. M., Liestøl, K., Raiborg, C., Campsteijn, C., & Stenmark, H. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201507009 · Cited by 163
Metadata
- Authors
- Bajorek, M., Schubert, H. L., McCullough, J., Langelier, C., Eckert, D. M., Stubblefield, W.-M. B., Uter, N. T., Myszka, D. G., Hill, C. P., & Sundquist, W. I.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-06-14
- Volume
- 16
- Issue
- 7
- Pages
- 754-762
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2089916390
- Cited by
- 224
- References
- 2
- FWCI
- 6.75
- Type
- journal article
- Language
- en
- Open access
- green
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- Bajorek, M., Schubert, H. L., McCullough, J., Langelier, C., Eckert, D. M., Stubblefield, W.-M. B., Uter, N. T., Myszka, D. G., Hill, C. P., & Sundquist, W. I. (2009). Structural basis for ESCRT-III protein autoinhibition. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1621
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