PAK2

P21 protein (Cdc42/Rac)-activated kinase 2
PDB rendering based on 1e0a.
Available structures PDB 1e0a, 1ees, 1f3m, 1yhv, 1yhw, 2hy8
Identifiers
Symbols	PAK2; PAK65; PAKgamma
External IDs	OMIM: 605022 MGI: 1339984 HomoloGene: 99711 GeneCards: PAK2 Gene
EC number	2.7.11.1
Gene Ontology Molecular function • nucleotide binding • protein kinase activity • protein serine/threonine kinase activity • protein binding • ATP binding • protein kinase binding • protein tyrosine kinase activator activity • identical protein binding Cellular component • nucleus • cytoplasm • cytosol • cytosol • plasma membrane • perinuclear region of cytoplasm Biological process • protein phosphorylation • negative regulation of protein kinase activity • apoptosis • cellular component disassembly involved in apoptosis • signal transduction • axon guidance • viral reproduction • peptidyl-serine phosphorylation • T cell costimulation • regulation of growth • regulation of apoptosis • interspecies interaction between organisms • protein autophosphorylation • regulation of defense response to virus by virus • positive regulation of peptidyl-tyrosine phosphorylation • T cell receptor signaling pathway • positive regulation of protein tyrosine kinase activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5062	224105
Ensembl	ENSG00000180370	ENSMUSG00000022781
UniProt	Q13177	Q5DTJ2
RefSeq (mRNA)	NM_002577.4	NM_177326.2
RefSeq (protein)	NP_002568.2	NP_796300.1
Location (UCSC)	Chr 3: 196.47 – 196.56 Mb	Chr 16: 32.02 – 32.08 Mb
PubMed search	[1]	[2]

Serine/threonine-protein kinase PAK 2 is an enzyme that in humans is encoded by the PAK2 gene.^[1][2]

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.^[3]

Interactions

PAK2 has been shown to interact with SH3KBP1,^[4] CDC42^[5][6][7] and Abl gene.^[8]

References

1. ^ Martin GA, Bollag G, McCormick F, Abo A (Jun 1995). "A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20". EMBO J 14 (9): 1970–8. PMC 398296. PMID 7744004. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=398296. 
2. ^ Knaus UG, Morris S, Dong HJ, Chernoff J, Bokoch GM (Aug 1995). "Regulation of human leukocyte p21-activated kinases through G protein--coupled receptors". Science 269 (5221): 221–3. doi:10.1126/science.7618083. PMID 7618083. 
3. ^ "Entrez Gene: PAK2 p21 (CDKN1A)-activated kinase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5062. 
4. ^ Kurakin, Alexei V; Wu Susan, Bredesen Dale E (Sep. 2003). "Atypical recognition consensus of CIN85/SETA/Ruk SH3 domains revealed by target-assisted iterative screening". J. Biol. Chem. (United States) 278 (36): 34102–9. doi:10.1074/jbc.M305264200. ISSN 0021-9258. PMID 12829691. 
5. ^ Stevens, W K; Vranken W, Goudreau N, Xiang H, Xu P, Ni F (May. 1999). "Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface". Biochemistry (UNITED STATES) 38 (19): 5968–75. doi:10.1021/bi990426u. ISSN 0006-2960. PMID 10320322. 
6. ^ Abo, A; Qu J, Cammarano M S, Dan C, Fritsch A, Baud V, Belisle B, Minden A (Nov. 1998). "PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia". EMBO J. (ENGLAND) 17 (22): 6527–40. doi:10.1093/emboj/17.22.6527. ISSN 0261-4189. PMC 1171000. PMID 9822598. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171000. 
7. ^ Zhang, B; Chernoff J, Zheng Y (Apr. 1998). "Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA". J. Biol. Chem. (UNITED STATES) 273 (15): 8776–82. doi:10.1074/jbc.273.15.8776. ISSN 0021-9258. PMID 9535855. 
8. ^ Roig, J; Tuazon P T, Zipfel P A, Pendergast A M, Traugh J A (Dec. 2000). "Functional interaction between c-Abl and the p21-activated protein kinase γ-PAK". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (26): 14346–51. doi:10.1073/pnas.97.26.14346. ISSN 0027-8424. PMC 18921. PMID 11121037. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18921. 

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. doi:10.1016/S0962-8924(99)01618-9. PMID 10461188. 
• Roig J, Traugh JA (2001). "Cytostatic p21 G protein-activated protein kinase gamma-PAK". Vitam. Horm.. Vitamins & Hormones 62: 167–98. doi:10.1016/S0083-6729(01)62004-1. ISBN 978-0-12-709862-3. 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. PMC 1083955. PMID 11463741. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1083955. 
• 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. doi:10.1007/BF02970151. 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. doi:10.2174/1389203043486955. PMID 14965316. 
• Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection". Curr. HIV Res. 3 (1): 87–94. doi:10.2174/1570162052773013. 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. PMC 394523. PMID 7556080. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=394523. 
• 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. doi:10.1074/jbc.270.36.21121. PMID 7673144. 
• 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. doi:10.1016/S1074-7613(00)80331-3. 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. PMC 191654. PMID 9151826. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=191654. 
• 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. doi:10.1016/S0960-9822(97)70091-5. 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. doi:10.1074/jbc.273.15.8776. 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. doi:10.1074/jbc.273.44.28733. 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. doi:10.1074/jbc.274.12.8022. PMID 10075701. 

External links

• PAK2 Info with links in the Cell Migration Gateway