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FEBS Lett. 2001 Oct 26;507(2):195-9.

Cdc42-independent activation and translocation of the cytostatic p21-activated protein kinase gamma-PAK by sphingosine.

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Department of Biochemistry, University of California, Riverside, CA 92521, USA.


Autophosphorylation of p21-activated protein kinase gamma-PAK is stimulated at 10 microM sphingosine in vitro and is maximal at 100 microM. Sites autophosphorylated on gamma-PAK in response to sphingosine are identical to those obtained with Cdc42(GTP). Autophosphorylation is paralleled by stimulation of gamma-PAK activity as measured with peptide and protein substrates. In 3T3-L1 cells, sphingosine stimulates the autophosphorylation and activity of gamma-PAK associated with the membrane-containing particulate fraction by 2.8-fold, but does not stimulate the activity of the soluble enzyme. Thus, gamma-PAK is activatable via a Cdc42-independent mechanism, suggesting sphingosine has a role in gamma-PAK activation under conditions of cell stress.

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