PAK2

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P21 (CDKN1A)-activated kinase 2
File:PBB Protein PAK2 image.jpg
PDB rendering based on 1e0a.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PAK2 ; PAK65; PAKgamma
External IDs Template:OMIM5 Template:MGI HomoloGene37639
RNA expression pattern
File:PBB GE PAK2 208875 s at tn.png
File:PBB GE PAK2 208876 s at tn.png
File:PBB GE PAK2 208877 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

P21 (CDKN1A)-activated kinase 2, also known as PAK2, is a human gene.

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.[1]

References

  1. "Entrez Gene: PAK2 p21 (CDKN1A)-activated kinase 2".

Further reading

  • Bokoch GM (1999). "Caspase-mediated activation of PAK2 during apoptosis: proteolytic kinase activation as a general mechanism of apoptotic signal transduction?". Cell Death Differ. 5 (8): 637–45. doi:10.1038/sj.cdd.4400405. PMID 10200518.
  • Bagrodia S, Cerione RA (1999). "Pak to the future". Trends Cell Biol. 9 (9): 350–5. PMID 10461188.
  • Roig J, Traugh JA (2001). "Cytostatic p21 G protein-activated protein kinase gamma-PAK". Vitam. Horm. 62: 167–98. PMID 11345898.
  • Geyer M, Fackler OT, Peterlin BM (2001). "Structure--function relationships in HIV-1 Nef". EMBO Rep. 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMID 11463741.
  • Greenway AL, Holloway G, McPhee DA; et al. (2004). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication". J. Biosci. 28 (3): 323–35. PMID 12734410.
  • Leavitt SA, SchOn A, Klein JC; et al. (2004). "Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm". Curr. Protein Pept. Sci. 5 (1): 1–8. PMID 14965316.
  • Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection". Curr. HIV Res. 3 (1): 87–94. PMID 15638726.
  • Quaranta MG, Mattioli B, Giordani L, Viora M (2006). "The immunoregulatory effects of HIV-1 Nef on dendritic cells and the pathogenesis of AIDS". FASEB J. 20 (13): 2198–208. doi:10.1096/fj.06-6260rev. PMID 17077296.
  • Brandon SD, Masaracchia RA (1991). "Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6". J. Biol. Chem. 266 (1): 380–5. PMID 1985906.
  • Martin GA, Bollag G, McCormick F, Abo A (1995). "A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20". EMBO J. 14 (17): 4385. PMID 7556080.
  • Knaus UG, Morris S, Dong HJ; et al. (1995). "Regulation of human leukocyte p21-activated kinases through G protein--coupled receptors". Science. 269 (5221): 221–3. PMID 7618083.
  • Benner GE, Dennis PB, Masaracchia RA (1995). "Activation of an S6/H4 kinase (PAK 65) from human placenta by intramolecular and intermolecular autophosphorylation". J. Biol. Chem. 270 (36): 21121–8. PMID 7673144.
  • Martin GA, Bollag G, McCormick F, Abo A (1995). "A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20". EMBO J. 14 (9): 1970–8. PMID 7744004.
  • Baur AS, Sass G, Laffert B; et al. (1997). "The N-terminus of Nef from HIV-1/SIV associates with a protein complex containing Lck and a serine kinase". Immunity. 6 (3): 283–91. PMID 9075929.
  • Swingler S, Gallay P, Camaur D; et al. (1997). "The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix". J. Virol. 71 (6): 4372–7. PMID 9151826.
  • Sells MA, Knaus UG, Bagrodia S; et al. (1997). "Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells". Curr. Biol. 7 (3): 202–10. PMID 9395435.
  • Zhang B, Chernoff J, Zheng Y (1998). "Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA". J. Biol. Chem. 273 (15): 8776–82. PMID 9535855.
  • Walter BN, Huang Z, Jakobi R; et al. (1998). "Cleavage and activation of p21-activated protein kinase gamma-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity". J. Biol. Chem. 273 (44): 28733–9. PMID 9786869.
  • Chew TL, Masaracchia RA, Goeckeler ZM, Wysolmerski RB (1999). "Phosphorylation of non-muscle myosin II regulatory light chain by p21-activated kinase (gamma-PAK)". J. Muscle Res. Cell. Motil. 19 (8): 839–54. PMID 10047984.
  • Gatti A, Huang Z, Tuazon PT, Traugh JA (1999). "Multisite autophosphorylation of p21-activated protein kinase gamma-PAK as a function of activation". J. Biol. Chem. 274 (12): 8022–8. PMID 10075701.

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