Abstract
p21-activated kinase (PAK) was the first identified serine/threonine protein kinase to bind and be activated by Rho GTPases. Since it was discovered some 10 years ago, PAK has been intensively studied and represents the best understood of the Rho-associated kinases. PAK family kinases are encoded by six mammalian genes with three conventional PAKs (PAK1–3) and three non-conventional PAKs (PAK4–6). Cdc42/Rac activates conventional PAKs through modulation of a kinase inhibitory (KI) domain by the overlapping Cdc42/Rac interaction/binding (CRIB) domain. Nonetheless PAKs can also be activated in GTPase independent manners, including by protease cleavage, translocation to membranes and binding to lipids. As a key signaling component, PAK is evolutionarily conserved from yeast to man. In mammalian cells PAKs play roles in many cellular signaling pathways such as the regulation of focal adhesion and actin dynamics, changes in cell morphology, cell motility, and the regulation of gene expression. Recently a number of studies show PAK is implicated disease states. As a result PAK family kinases are becoming good candidates for drug development.
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Zhao, ZS. (2005). The Prototype Rho-Associated Kinase PAK. In: Manser, E. (eds) RHO Family GTPases. Proteins and Cell Regulation, vol 3. Springer, Dordrecht. https://doi.org/10.1007/1-4020-3462-8_10
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DOI: https://doi.org/10.1007/1-4020-3462-8_10
Publisher Name: Springer, Dordrecht
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