The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
A purified Drosophila septin complex forms filaments and exhibits GTPase activity.
Open accessAbstract
Septin proteins are necessary for cytokinesis in budding yeast and Drosophila and are thought to be the subunits of the yeast neck filaments. To test whether septins actually form filaments, an immunoaffinity approach was used to isolate a septin complex from Drosophila embryos. The purified complex is comprised of the three previously identified septin polypeptides Pnut, Sep2, and Sep1. Hydrodynamic and sequence data suggest that the complex is composed of a heterotrimer of homodimers. The complex copurifies with one molecule of bound guanine nucleotide per septin polypeptide. It binds and hydrolyzes exogenously added GTP. These observations together with conserved sequence motifs identify the septins as members of the GTPase superfamily. We discuss a model of filament structure and speculate as to how the filaments are organized within cells.
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Cites
Predicting coiled coils from protein sequences.
Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
Cited by
Self- and actin-templated assembly of Mammalian septins
Kinoshita, M., Field, C. M., Coughlin, M. L., Straight, A. F., & Mitchison, T. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00366-0 · Cited by 526
Structural insight into filament formation by mammalian septins
Sirajuddin, M., Farkasovsky, M., Hauer, F., Kühlmann, D., Macara, I. G., Weyand, M., Stark, H., & Wittinghofer, A. (2007) · Nature · doi:10.1038/nature06052 · Cited by 481
The pathobiology of the septin gene family
Hall, P. A., & Russell, S. H. (2004) · The Journal of Pathology · doi:10.1002/path.1654 · Cited by 323
Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli
Mukherjee, A., Cao, C., & Lutkenhaus, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.2885 · Cited by 247
Field, C. M., Coughlin, M., Doberstein, S., Marty, T., & Sullivan, W. (2005) · Development · doi:10.1242/dev.01843 · Cited by 156
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Metadata
- Authors
- Field, C. M., al-Awar, O., Rosenblatt, J., Wong, M. L., Alberts, B., & Mitchison, T. J.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1996-05-01
- Volume
- 133
- Issue
- 3
- Pages
- 605-616
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2098616171
- Cited by
- 326
- References
- 2
- FWCI
- 6.82
- Type
- journal article
- Language
- en
- Open access
- green
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- Field, C. M., al-Awar, O., Rosenblatt, J., Wong, M. L., Alberts, B., & Mitchison, T. J. (1996). A purified Drosophila septin complex forms filaments and exhibits GTPase activity. The Journal of cell biology. https://doi.org/10.1083/jcb.133.3.605
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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