PAK2

From Wikipedia, the free encyclopedia

P21 (CDKN1A)-activated kinase 2

PDB rendering based on 1e0a.

Available structures: 1e0a, 1ees, 1f3m, 1yhv, 1yhw, 2hy8

Identifiers

Symbol(s)

PAK2; PAK65; PAKgamma

External IDs

OMIM: 605022 MGI: 1339984 HomoloGene: 37639

Gene ontology
Molecular Function:	• nucleotide binding • structural constituent of ribosome • protein serine/threonine kinase activity • protein binding • ATP binding • transferase activity
Cellular Component:	• intracellular • ribosome
Biological Process:	• translation • protein amino acid phosphorylation • negative regulation of protein kinase activity • signal transduction • protein amino acid autophosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

XM_001126110 (mRNA)
XP_001126110 (protein)

NM_177326 (mRNA)
NP_796300 (protein)

Location

Chr 3: 197.95 - 198.04 Mb

Chr 16: 31.94 - 32 Mb

Pubmed search

[1]

[2]

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]

[edit] References

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

[edit] 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.