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Title: Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family
Authors: Manser, E. 
Chong, C. 
Zhao, Z.-S. 
Leung, T. 
Michael, G. 
Hall, C.
Lim, L.
Issue Date: 1995
Citation: Manser, E., Chong, C., Zhao, Z.-S., Leung, T., Michael, G., Hall, C., Lim, L. (1995). Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family. Journal of Biological Chemistry 270 (42) : 25070-25078. ScholarBank@NUS Repository.
Abstract: A number of 'target' proteins for the Rho family of small GTP-binding proteins have now been identified, including the protein kinases ACK and p65(PAK) (Manser, E., Leung, T., Salihuddin, H, Zhao, Z.-S., and Lim, L. (1994) Nature 367, 40-46). The purified serine/threonine kinase p65(PAK) has been shown to be directly activated by GTP-Rac1 or GTP-Cdc42. Here we report the cDNA sequence encoding a new brain-enriched PAK isoform β-PAK, which shares 79% amino acid identity with the previously described α-isoform. Their mRNAs are differentially expressed in the brain, with α-PAK mRNA being particularly abundant in motor-associated regions. In vitro translation products of the α- and β-PAK cDNAs exhibited relative molecular masses of 68,000 and 65,000, respectively, by SDS-polyacrylamide analysis. A specific β-PAK peptide sequence was obtained from rat brain-purified p65(PAK). Recombinant α- and β-PAKs exhibited an increase in kinase activity mediated by GTP-p21 induced autophosphorylation. Cdc42 was a more potent activator in vitro of α-PAK kinase, and the fully activated enzyme is 300 times more active than the unphosphorylated form. Interestingly the down-regulation in the binding of p21s to recombinant β-PAK and brain p65(PAK) which is observed upon kinase activation does not occur with recombinant α-PAK.
Source Title: Journal of Biological Chemistry
ISSN: 00219258
DOI: 10.1074/jbc.270.42.25070
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