Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation (   ). Acts as a downstream effector of the small GTPases CDC42 and RAC1 . Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues . Full-length PAK2 stimulates cell survival and cell growth . Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration . Phosphorylates JUN and plays an important role in EGF-induced cell proliferation . Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP . Phosphorylates CASP7, thereby preventing its activity (, ). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (, ). On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway ( ). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation .
Subcellular locations: Cytoplasm, Nucleus
MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane.
Subcellular locations: Nucleus, Cytoplasm, Perinuclear region, Membrane
Interaction with ARHGAP10 probably changes PAK-2p34 location to cytoplasmic perinuclear region . Myristoylation changes PAK-2p34 location to the membrane .
Ubiquitously expressed. Higher levels seen in skeletal muscle, ovary, thymus and spleen.