p21-activated kinase 6 (PAK6) is a member of the PAK family of serine/threonine kinases. These kinases have a highly conserved amino-terminal Cdc42/Rac interactive binding domain and a carboxyl-terminal kinase domain. PAK kinases are implicated in the regulation of a number of cellular processes, including cytoskeleton rearrangement, apoptosis and the MAP kinase signaling pathway. PAK6 interacts with the androgen receptor, a steroid hormone transcription factor involved in male sexual differentiation and development. PAK6 is highly expressed in testis and prostate tissues. Regulation of PAK6 kinase activity occurs through multiple sites of phosphorylation. Activation of PAK6 requires autophosphorylation of Ser-560 and MKK-6 induced phosphorylation of Tyr-566. In addition, p38 MAPK can phosphorylate Ser-165, which increases PAK6 kinase activity. Thus, multiple signaling pathways may regulate the activity of PAK6 through differential phosphorylation.
Schrantz, N. et al. (2004) J. Biol. Chem. 279(3):1922.
Lee, S.R. et al. (2002) Mol. Endocrin. 16(1):85.
*For more information, see UniProt Accession Q9NQU5
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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