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Structure of small G proteins and their regulators Paduch M; Jelen F; Otlewski JActa Biochim Pol 2001[]; 48 (4): 829-50In recent years small G proteins have become an intensively studied group of regulatory GTP hydrolases involved in cell signaling. More than 100 small G proteins have been identified in eucaryotes from protozoan to human. The small G protein superfamily includes Ras, Rho Rab, Rac, Sarl/Arf and Ran homologs, which take part in numerous and diverse cellular processes, such as gene expression, cytoskeleton reorganization, microtubule organization, and vesicular and nuclear transport. These proteins share a common structural core, described as the G domain, and significant sequence similarity. In this paper we review the available data on G domain structure, together with a detailed analysis of the mechanism of action. We also present small G protein regulators: GTPase activating proteins that bind to a catalytic G domain and increase its low intrinsic hydrolase activity, GTPase dissociation inhibitors that stabilize the GDP-bound, inactive state of G proteins, and guanine nucleotide exchange factors that accelerate nucleotide exchange in response to cellular signals. Additionally, in this paper we describe some aspects of small G protein interactions with down-stream effectors.|Amino Acid Sequence[MESH]|GTP Phosphohydrolases/metabolism[MESH]|GTP-Binding Proteins/*chemistry[MESH]|Humans[MESH]|Hydrolysis[MESH]|Models, Chemical[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Protein Conformation[MESH]|Protein Structure, Tertiary[MESH]|Sequence Homology, Amino Acid[MESH]|Signal Transduction[MESH] |
