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Gβγ subunits stimulate p21‐activated kinase 1 (PAK1) through activation of PI3‐kinase and Akt but act independently of Rac1/Cdc42
Author(s) -
Menard Raymond E,
Mattingly Raymond R
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01406-6
Subject(s) - pak1 , wortmannin , rac1 , cdc42 , microbiology and biotechnology , phosphoinositide 3 kinase , protein kinase b , kinase , chemistry , ask1 , cyclin dependent kinase 2 , signal transduction , biology , protein kinase a
The p21‐activated kinase (PAK) family is homologous to the yeast sterile 20 (Ste20) and regulates a wide variety of cellular responses, including cell morphology, proliferation, and survival. In this study we examined the activation of PAK1 by Gβγ subunits. Co‐transfection of COS7 cells with Gβ1γ2 or Gβ1γ5 was sufficient to induce agonist‐independent activation of PAK1. Expression of dominant/negative Rac, Cdc42, or Ras did not inhibit this Gβγ‐dependent activation. Wortmannin, which inhibits phosphoinositide 3‐kinase (PI3‐kinase) activity, and expression of a dominant/negative form of Akt were sufficient to abrogate the activation of PAK1 that was induced by Gβγ. These results reveal that stimulation of PAK1 by Gβγ can occur via a PI3‐kinase and Akt pathway that does not require Rac1 or Cdc42.