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Background: p21-activated kinase 2 (PAK2) is a member of a family of serine/threonine protein kinase defined by their interaction with the small GTPases, Cdc42 and Rac (1-2). The PAK proteins can be essentially divided into two categories, groups I (PAK1, PAK2 and PAK3) and group II (PAK4, PAK5 and PAK6), based on their structures (3). All six PAKs play an important role in diverse cellular processes, including cytoskeletal dynamics, growth/apoptotic signal transduction through MAP kinases, and regulation of transcription factors (4). PAK2 is unique among the PAK isoforms because it is also activated through proteolytic cleavage by caspases or caspase-like proteases (5). Full-length PAK-2 is localized in the cytoplasm, whereas the proteolytic PAK-2p34 fragment translocates to the nucleus. Activation of full-length PAK-2 stimulates cell survival, and proteolytic activation of PAK-2p34 is involved in programmed cell death (6). Phosphorylation within the Nck (Serine 20) and Pak-interacting guanine nucleotide exchange factor (Serine 192 and Serine 197) binding sites blocks the interactions of Pak 2 with certain proteins (7).