The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A
Open accessAbstract
The VPS4 AAA ATPases function both in endosomal vesicle formation and in the budding of many enveloped RNA viruses, including HIV-1. VPS4 proteins act by binding and catalyzing release of the membrane-associated ESCRT-III protein lattice, thereby allowing multiple rounds of protein sorting and vesicle formation. Here, we report the solution structure of the N-terminal VPS4A m icrotubule i nteracting and t ransport (MIT) domain and demonstrate that the VPS4A MIT domain binds the C-terminal half of the ESCRT-III protein, CHMP1B ( K d = 20 ± 13 μM). The MIT domain forms an asymmetric three-helix bundle that resembles the first three helices in a tetratricopeptide repeat (TPR) motif. Unusual interhelical interactions are mediated by a series of conserved aromatic residues that form coiled-coil interactions between the second two helices and also pack against the conserved alanines that interdigitate between the first two helices. Mutational analyses revealed that a conserved leucine residue (Leu-64) on the third helix that would normally bind the fourth helix in an extended TPR is used to bind CHMP1B, raising the possibility that ESCRT-III proteins may bind by completing the TPR motif.
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Cites
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., Morham, S. G., Zavitz, K. H., Wang, H. E., Wettstein, D. A., Stray, K. M., Côté, M., Rich, R. L., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00506-2 · Cited by 1,369
Self-citationFunctional Surfaces of the Human Immunodeficiency Virus Type 1 Capsid Protein
von Schwedler, U. K., Stray, K. M., Garrus, J. E., & Sundquist, W. I. (2003) · Journal of Virology · doi:10.1128/jvi.77.9.5439-5450.2003 · Cited by 421
Self-citationWalshaw, J., & Woolfson, D. N. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4545 · Cited by 357
Schubert, M., Labudde, D., Oschkinat, H., & Schmieder, P. (2002) · Journal of Biomolecular NMR · doi:10.1023/a:1020997118364 · Cited by 351
Cited by
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
THE ESCRT COMPLEXES: Structure and Mechanism of a Membrane-Trafficking Network
Hurley, J. H., & Emr, S. D. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102126 · Cited by 546
The Molecular Mechanism of Hepcidin-mediated Ferroportin Down-Regulation
De Domenico, I., Ward, D. M., Langelier, C., Vaughn, M. B., Nemeth, E., Sundquist, W. I., Ganz, T., Musci, G., & Kaplan, J. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-01-0060 · Cited by 434
Self-citationPlasma 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
Teasdale, R. D., & Collins, B. M. (2012) · Biochemical Journal · doi:10.1042/bj20111226 · Cited by 281
Metadata
- Authors
- Scott, A., Gaspar, J., Stuchell-Brereton, M. D., Alam, S. L., Skalicky, J. J., & Sundquist, W. I.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-09-20
- Volume
- 102
- Issue
- 39
- Pages
- 13813-13818
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2059494185
- Cited by
- 182
- References
- 7
- FWCI
- 7.17
- Type
- journal article
- Language
- en
- Open access
- green
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