PAK5: Human p21 activated kinase 5
PDB Code: 2F57
The p21-activated protein kinases (PAKs) are serine/threonine protein kinases of the STE20 family which are involved in Cdc42 and Rac1 signaling. PAK kinases contain a well defined p21-binding domain (PBD) including the CRIB motif. Six members of this kinase family have been identified in human. The PAK kinase family is subdivided into two groups according to kinase domain homology and the existence of a conserved autoinhibitory domain (AID). Group I PAKs (PAKs 1, 2, and 3) exhibit 80 to 90% sequence identity within their catalytic domains and contain a AID domain, whereas the recently identified group II PAKs (PAK 4, 5, and 6), share only about 40 to 50% identity to group I kinase domains and do not contain obvious AID domains. Thus, the mechanisms that regulate group II PAKs are unclear, but the absence of a conserved AID indicates that the modes of regulation differ significantly from group I PAKs.
PAK5 is highly expressed in the brain and neuronal tissues and is expressed at lower levels in several other tissues such as liver, kidney and heart. PAK5, unlike PAK1, cannot complement an STE 20 mutation in Saccharomyces cerevisiae . PAK5 has been shown to bind GTPases Cdc42 and Rac, but these GTPases do not regulate PAK5 kinase activity, which is constitutively active and has a higher specific activity than any other PAK family member. PAK5 is localized to mitochondria, and localization is independent of kinase activity or Cdc42 binding.
Knockout mice of PAK5 show no apparent phenotype potentially due to functional redundancy with other PAKs. However, PAK5 has been shown to be an important mediator in the signaling pathway by which Rho GTPases control cytoskeletal changes necessary for promoting neurite outgrowth. Similar to other Group II PAKs, PAK5 is activated by MKK6, consistent with the presence of a conserved TPY motif in the activation domain. PAK5 prevents apoptosis induced by camptothecin and C2-ceramide by phosphorylating BAD ( BCL 2-antagonist of cell death) on Ser-112 in a protein kinase A-independent manner and prevents the localization of BAD to mitochondria, thereby inhibiting the apoptotic cascade. PAK5 has also been to keep microtubules stable through down regulation of MARK2 but ir destabilizes the F-actin network so that stress fibers and focal adhesions disappear and cells develop filopodia.
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