Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.270.42.25070
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. https://doi.org/10.1074/jbc.270.42.25070
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
URI: http://scholarbank.nus.edu.sg/handle/10635/115815
ISSN: 00219258
DOI: 10.1074/jbc.270.42.25070
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

202
checked on Oct 12, 2021

WEB OF SCIENCETM
Citations

211
checked on Oct 12, 2021

Page view(s)

85
checked on Oct 14, 2021

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.