The structure of the GTPase-activating domain from p50rhoGAP
Article Abstract:
Rho proteins transduce signals from plasma-membrane receptors; regulate cell adhesion, motility and shape through actin cytoskeleton formation; stimulate other kinases cascades; and serve as molecular switches. They have an active GTP-bound form supported by guanine-nucleotide exchange factors, as well as an inactive GTP-bound form supported by GTPase-activating proteins (GAP) that promote inherent GTPase activity of small G proteins. An active 242-residue C-terminal fragment of human p50rhoGAP is described in terms of its crystal structure.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Role for the Rho-family GTPase Cdc42 in yeast mating-pheromone signal pathway
Article Abstract:
The highly conserved human homolog of Cdc42 in the GTP-bound form binds and activates a protein kinase, PAK65, that has a sequence similar to Ste20. Cdc42 also shows the ability to promote protein kinase activity of Ste20. The Cdc24 and Cdc42 proteins seem to belong to the primary mating-pheromone signal-transduction pathway. The role of GTPase in linking cell differentiation to morphogenetic processes is discussed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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A yeast GTPase-activating protein that interacts specifically with a member of the Ypt/Rab family
Article Abstract:
A yeast GTPase-activating protein has been cloned for the Ypt/Rab family of proteins. The gene is GTP6 which encodes a protein that is highly specific for the Ypt6 protein. The exact function of the Ypt6 protein has not been elucidated, but evidence suggests it is involved in vacuolar protein sorting or transport.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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