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Validated All-in-One™ qPCR Primer for PAK2(NM_002577.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
The p21 activated kinases (PAK) are critical effectors that link Rho GTPases to cytoskeleton reorganization and nuclear signaling. The PAK proteins are a family of serine/threonine kinases that serve as targets for the small GTP binding proteins, CDC42 and RAC1, and have been implicated in a wide range of biological activities. The protein encoded by this gene is activated by proteolytic cleavage during caspase-mediated apoptosis, and may play a role in regulating the apoptotic events in the dying cell. [provided by RefSeq].
Gene References into function
- Cdc42/Rac1-dependent activation of PAK may trigger early platelet shape change, at least in part through the regulation of cortactin binding to PAK.
- The enzymatic phosphorylation reaction of PAK2 can be best interpreted by a rapid-equilibrium random bi-bi reaction model; the catalysis reaction is partially limited by both the phosphoryl group transfer and the product release steps.
- The opposing effects of Core protein on the transcription pf P21 might be important in the progression of liver disease in HCV-positive patients.
- Caspase-activated PAK-2 is regulated by subcellular targeting and proteasomal degradation
- sites of PAK2 autophosphorylation in the regulatory and the catalytic domains and their kinetic effect; multiple regions of PAK2 are involved in the enzyme-substrate recognition
- Pak2 phosphorylates Myc at three sites (T358, S373, and T400) and affects Myc functions both in vitro and in vivo
- Nef induces signal transduction via the recruitment of a signaling machinery including Pak2 into lipid rafts, thereby mimicking a physiological cellular mechanism to initiate the TCR cascade.
- PAK2 is constitutively activated in certain breast cancer cell lines and that this active PAK is mislocalized to atypical focal adhesions in the absence of high levels of activated Rho GTPases.
- PAK2 kinase activity is increased in response to TCR stimulation; results suggest a novel role for PAK2 as a positive regulator of T cell activation.
- interacts with Nef proteins from SIV infected chimpanzees
- Pak2 has a role in the down-regulation of translation initiation in apoptosis by phosphorylation of Mnk1
- PS-GAP is a novel regulator of caspase-activated PAK-2
- PAK-2 is activated in 1-LN prostate cancer cells by a proteinase inhibitor, alpha 2-macroglobulin
- binding of Cdc42 localizes Pak2 to the endoplasmic reticulum, where autophosphorylation alters association of the two proteins
- Pak2 binds to and phosphorylates initiation factor eIF4G, which inhibits association of eIF4E with m7GTP, reducing translation initiation.
- Nef protein amino acids at positions 85, 89, 187, 188, and 191 (L, H, S, R, and F in the clade B consensus, respectively) are critical for Pak2 association and activation
- Posttranslational myristoylation of PAK2 might be part of a unique series of mechanisms involved in the regulation of the later events of apoptosis.
- c-Abl represents a target downstream of phosphatidylinositol 3-kinase-activated PAK2, which differentiates TGF-beta signaling in fibroblasts and epithelial cell lines.
- This study of tissue-derived HIV-1 Nefs demonstrates that CD4 and MHC-I downregulation are highly conserved Nef functions, while Pak2 association is variable in late stage AIDS patients.
- define a new class of PAK-interacting proteins, which play an important role in actin cytoskeletal reorganization
- bring novel insights into our understanding of synergistic regulation of MUC5AC mucin by both pathological and physiological inducers
- interaction of Nef with PAK2 does not play a major role in T-cell activation, viral replication, and apoptosis.
- protein phosphatase 1alpha can act directly on phosphorylated Thr-402 in the activation loop of PAK2 and down-regulate its kinase activity
- Data show RNAi-mediated or dominant-negative suppression of Pak2, major regulators of cytoskeletal signaling downstream of Cdc42 or Rac1, markedly inhibits EC lumen and tube formation.
- Clathrin-independent endocytosis used by the IL-2 receptor is regulated by Rac1, Pak1 and Pak2.
- Pak1 and Pak2 mediate tumor cell invasion through distinct signaling mechanisms
