Always look on the bright site of Rho: structural implications for a conserved intermolecular interface
Open Access
- 1 December 2004
- journal article
- review article
- Published by Springer Science and Business Media LLC in EMBO Reports
- Vol. 5 (12), 1130-1136
- https://doi.org/10.1038/sj.embor.7400293
Abstract
The signalling functions of Rho‐family GTPases are based on the formation of distinctive protein–protein complexes. Invaluable insights into the structure–function relationships of the Rho GTPases have been obtained through the resolution of several of their structures in complex with regulators and downstream effectors. In this review, we use these complexes to compare the binding and specificity‐determining sites of the Rho GTPases. Although the properties that characterize these sites are diverse, some fundamental conserved principles that govern their intermolecular interactions have emerged. Notably, all of the interacting partners of the Rho GTPases, irrespective of their function, bind to a common set of conserved amino acids that are clustered on the surface of the switch regions. This conserved region and its specific structural characteristics exemplify the convergence of the Rho GTPases on a consensus binding site.Keywords
This publication has 52 references indexed in Scilit:
- Models of the Cooperative Mechanism for Rho Effector RecognitionPublished by Elsevier BV ,2004
- An activating mutant of Rac1 that fails to interact with Rho GDP-dissociation inhibitor stimulates membrane ruffling in mammalian cellsBiochemical Journal, 2004
- Structural Elements, Mechanism, and Evolutionary Convergence of Rho Protein−Guanine Nucleotide Exchange Factor ComplexesBiochemistry, 2003
- Switch-of-Function Mutants Based on Morphology Classification of Ras Superfamily Small GTPasesCell, 2003
- Rho GTPases in cell biologyNature, 2002
- Structural basis for the selective activation of Rho GTPases by Dbl exchange factorsNature Structural & Molecular Biology, 2002
- The Guanine Nucleotide-Binding Switch in Three DimensionsScience, 2001
- Structure of the Complex of Cdc42Hs with a Peptide Derived from P-21 Activated Kinase,Biochemistry, 2000
- How RhoGDI binds RhoActa Crystallographica Section D-Structural Biology, 1999
- Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAPNature Structural & Molecular Biology, 1998