The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Comparative functional analysis of the Rac GTPases
Abstract
Small GTPases of the Rho family including Rac, Rho and Cdc42 regulate different cellular processes like reorganization of the actin cytoskeleton by acting as molecular switches. The three distinct mammalian Rac proteins share very high sequence identity but how their specificity is achieved is hitherto unknown. Here we show that Rac1 and Rac3 are very closely related concerning their biochemical properties, such as effector interaction, nucleotide binding and hydrolysis. In contrast, Rac2 displays a slower nucleotide association and is more efficiently activated by the Rac‐GEF Tiam1. Modeling and normal mode analysis support the idea that altered dynamics of Rac2 at the switch I region may be responsible for different biochemical properties. These results provide insight into the individual functionalities of the Rac isoforms.
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“Activation generally requires release of inactive, guanosine diphosphate (GDP)-bound RAC2 from a guanine nucleotide dissociation inhibitor (GDI), RhoGDI, followed by association with a guanine exchange factor (GEF), such as TIAM1.10”
From Dominant activating RAC2 mutation with lymphopenia, immunodeficiency, and cytoskeletal defects (2019) · cites this paper as [10]
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Cites
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Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1
Worthylake, D. K., Rossman, K. L., & Sondek, J. (2000) · Nature · doi:10.1038/35047014 · Cited by 355
Trp56 of Rac1 Specifies Interaction with a Subset of Guanine Nucleotide Exchange Factors
Gao, Y., Xing, J., Streuli, M., Leto, T. L., & Zheng, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108865200 · Cited by 115
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Cited by
Deciphering the Molecular and Functional Basis of Dbl Family Proteins
Jaiswal, M., Dvorsky, R., & Ahmadian, M. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.429746 · Cited by 108
Self-citationDominant activating RAC2 mutation with lymphopenia, immunodeficiency, and cytoskeletal defects
Hsu, A. P., Donkó, A., Arrington, M. E., Swamydas, M., Fink, D., Das, A., Escobedo, O., Bonagura, V., Szabolcs, P., Steinberg, H. N., et al. (2019) · Blood · doi:10.1182/blood-2018-11-886028 · Cited by 92
Isozyme-specific stimulation of phospholipase C-γ2 by Rac GTPases
Piechulek, T., Rehlen, T., Walliser, C., Vatter, P., Moepps, B., & Gierschik, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509396200 · Cited by 80
Jaiswal, M., Gremer, L., Dvorsky, R., Haeusler, L. C., Cirstea, I. C., Uhlenbrock, K., & Ahmadian, M. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.226431 · Cited by 68
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Metadata
- Authors
- Haeusler, L. C., Blumenstein, L., Stege, P., Dvorsky, R., & Ahmadian, M. R.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2003-11-26
- Volume
- 555
- Issue
- 3
- Pages
- 556-560
- ISSN
- 0014-5793
- 1873-3468
- Cited by
- 68
- References
- 3
- Language
- en
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- Haeusler, L. C., Blumenstein, L., Stege, P., Dvorsky, R., & Ahmadian, M. R. (2003). Comparative functional analysis of the Rac GTPases. FEBS Letters. https://doi.org/10.1016/s0014-5793(03)01351-6
