First Author | Bagrodia S | Year | 1995 |
Journal | J Biol Chem | Volume | 270 |
Issue | 39 | Pages | 22731-7 |
PubMed ID | 7559398 | Mgi Jnum | J:29051 |
Mgi Id | MGI:76575 | Doi | 10.1074/jbc.270.39.22731 |
Citation | Bagrodia S, et al. (1995) Identification of a mouse p21Cdc42/Rac activated kinase [published erratum appears in J Biol Chem 1996 Jan 12;271(2):1250]. J Biol Chem 270(39):22731-7 |
abstractText | We have isolated a novel member of the mammalian PAK (p21 activated kinase) and yeast Ste20 serine/threonine kinase family from a mouse fibroblast cDNA library, designated mPAK-3. Expression of mPAK-3 in Saccharomyces cerevisiae partially restores mating function in ste20 null cells. Like other PAKs, mPAK-3 contains a putative Cdc42Hs/Rac binding sequence and when transiently expressed in COS cells, full-length mPAK-3 binds activated (GTP gamma S (guanosine 5'-3-O-(thio-triphosphate)-bound) glutathione S-transferase (GST)-Cdc42Hs and GST-Rac1 but not GST-RhoA. As expected for a putative target molecule, mPAK-3 does not bind to an effector domain mutant of Cdc42Hs. Furthermore, activated His-tagged Cdc42Hs and His-tagged Rac stimulate mPAK-3 autophosphorylation and phosphorylation of myelin basic protein by mPAK-3 in vitro. Interestingly, the amino-terminal region of mPAK-3 contains potential SH3-binding sites and we find that mPAK-3, expressed in vitro and in vivo, shows highly specific binding to the SH3 domain of phospholipase C-gamma and at least one SH3 domain in the adapter protein Nck. These results raise the possibility of an additional level of regulation of the PAK family in vivo. |