Abstract
Major advances have been made in understanding the structure, function and regulation of the small GTP-binding proteins of the Rho family and their involvement in multiple cellular process and disorders. However, intrinsic nucleotide exchange and hydrolysis reactions, which are known to be fundamental to Rho family proteins, have been partially investigated in the case of RhoA, Rac1 and Cdc42, but for others not at all. Here we present a comprehensive and quantitative analysis of the molecular switch functions of 15 members of the Rho family that enabled us to propose an active GTP-bound state for the rather uncharacterized isoforms RhoD and Rif under equilibrium and quiescent conditions.
©2012 by Walter de Gruyter Berlin Boston
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Artikel in diesem Heft
- Masthead
- Masthead
- Reviews
- Exosomes: the ideal nanovectors for biodelivery
- Biological applications of the electrochemical sensing of nitric oxide: fundamentals and recent developments
- Minireview
- Cerebral cavernous malformation is a vascular disease associated with activated RhoA signaling
- Research Articles/Short Communications
- Protein Structure and Function
- Diversity, abundance, and sex-specific expression of chemosensory proteins in the reproductive organs of the locust Locusta migratoria manilensis
- Structure of the Ca2+-saturated C-terminal domain of scallop troponin C in complex with a troponin I fragment
- An acetylation site in lectin domain modulates the biological activity of polypeptide GalNAc-transferase-2
- Reengineering of subtilisin Carlsberg for oxidative resistance
- New insight into the molecular switch mechanism of human Rho family proteins: shifting a paradigm
- Cell Biology and Signaling
- HbG200-mediated preinduction of heme oxygenase-1 improves bile flow and ameliorates pericentral downregulation of Bsep and Mrp2 following experimental liver ischemia and reperfusion
- Effect of silver nanoparticles on human primary keratinocytes
- Multifunctional silica nanoparticles for optical and magnetic resonance imaging
- Proteolysis
- Activation profiles of human kallikrein-related peptidases by matrix metalloproteinases