PAK3

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P21 (CDKN1A)-activated kinase 3
File:PBB Protein PAK3 image.jpg
PDB rendering based on 1e0a.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PAK3 ; CDKN1A; MRX30; MRX47; OPHN3; PAK3beta; bPAK; hPAK3
External IDs Template:OMIM5 Template:MGI HomoloGene: 55664
RNA expression pattern
File:PBB GE PAK3 214607 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 3, also known as PAK3, is a human gene.[1]

PAK proteins are critical effectors that link Rho GTPases to cytoskeleton reorganization and nuclear signaling. PAK proteins, a family of serine/threonine p21-activating kinases, serve as targets for the small GTP binding proteins Cdc42 and RAC and have been implicated in a wide range of biological activities. The protein encoded by this gene forms an activated complex with GTP-bound RAS-like (P21), CDC2 and RAC1 proteins which then catalyzes a variety of targets. This protein may be necessary for dendritic development and for the rapid cytoskeletal reorganization in dendritic spines associated with synaptic plasticity. A point mutation in this gene has been linked to nonsyndromic X-linked mental retardation.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: PAK3 p21 (CDKN1A)-activated kinase 3".

Further reading

  • Bagrodia S, Cerione RA (1999). "Pak to the future". Trends Cell Biol. 9 (9): 350–5. PMID 10461188.
  • Illarioshkin SN, Tanaka H, Markova ED; et al. (1996). "X-linked nonprogressive congenital cerebellar hypoplasia: clinical description and mapping to chromosome Xq". Ann. Neurol. 40 (1): 75–83. doi:10.1002/ana.410400113. PMID 8687195.
  • Donnelly AJ, Partington MW, Ryan AK, Mulley JC (1996). "Regional localisation of two non-specific X-linked mental retardation genes (MRX30 and MRX31)". Am. J. Med. Genet. 64 (1): 113–20. doi:10.1002/(SICI)1096-8628(19960712)64:1<113::AID-AJMG19>3.0.CO;2-Q. PMID 8826460.
  • Siow YL, Kalmar GB, Sanghera JS; et al. (1997). "Identification of two essential phosphorylated threonine residues in the catalytic domain of Mekk1. Indirect activation by Pak3 and protein kinase C.". J. Biol. Chem. 272 (12): 7586–94. PMID 9065412.
  • Diaz B, Barnard D, Filson A; et al. (1997). "Phosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biological signaling". Mol. Cell. Biol. 17 (8): 4509–16. PMID 9234708.
  • des Portes V, Soufir N, Carrié A; et al. (1997). "Gene for nonspecific X-linked mental retardation (MRX 47) is located in Xq22.3-q24". Am. J. Med. Genet. 72 (3): 324–8. PMID 9332663.
  • Manser E, Loo TH, Koh CG; et al. (1998). "PAK kinases are directly coupled to the PIX family of nucleotide exchange factors". Mol. Cell. 1 (2): 183–92. PMID 9659915.
  • Van Eyk JE, Arrell DK, Foster DB; et al. (1998). "Different molecular mechanisms for Rho family GTPase-dependent, Ca2+-independent contraction of smooth muscle". J. Biol. Chem. 273 (36): 23433–9. PMID 9722579.
  • Bagrodia S, Taylor SJ, Jordon KA; et al. (1998). "A novel regulator of p21-activated kinases". J. Biol. Chem. 273 (37): 23633–6. PMID 9726964.
  • Allen KM, Gleeson JG, Bagrodia S; et al. (1998). "PAK3 mutation in nonsyndromic X-linked mental retardation". Nat. Genet. 20 (1): 25–30. doi:10.1038/1675. PMID 9731525.
  • King AJ, Sun H, Diaz B; et al. (1998). "The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338". Nature. 396 (6707): 180–3. doi:10.1038/24184. PMID 9823899.
  • Mason CS, Springer CJ, Cooper RG; et al. (1999). "Serine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activation". EMBO J. 18 (8): 2137–48. doi:10.1093/emboj/18.8.2137. PMID 10205168.
  • Premont RT, Claing A, Vitale N; et al. (2000). "The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing". J. Biol. Chem. 275 (29): 22373–80. PMID 10896954.
  • Bienvenu T, des Portes V, McDonell N; et al. (2001). "Missense mutation in PAK3, R67C, causes X-linked nonspecific mental retardation". Am. J. Med. Genet. 93 (4): 294–8. PMID 10946356.
  • Hashimoto S, Tsubouchi A, Mazaki Y, Sabe H (2001). "Interaction of paxillin with p21-activated Kinase (PAK). Association of paxillin alpha with the kinase-inactive and the Cdc42-activated forms of PAK3". J. Biol. Chem. 276 (8): 6037–45. doi:10.1074/jbc.M005854200. PMID 11096073.
  • Chiloeches A, Mason CS, Marais R (2001). "S338 phosphorylation of Raf-1 is independent of phosphatidylinositol 3-kinase and Pak3". Mol. Cell. Biol. 21 (7): 2423–34. doi:10.1128/MCB.21.7.2423-2434.2001. PMID 11259591.
  • Chong C, Tan L, Lim L, Manser E (2001). "The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity". J. Biol. Chem. 276 (20): 17347–53. doi:10.1074/jbc.M009316200. PMID 11278486.
  • Stoletov KV, Ratcliffe KE, Spring SC, Terman BI (2001). "NCK and PAK participate in the signaling pathway by which vascular endothelial growth factor stimulates the assembly of focal adhesions". J. Biol. Chem. 276 (25): 22748–55. doi:10.1074/jbc.M009720200. PMID 11278553.
  • Yoshimura M, Homma K, Saito J; et al. (2001). "Dual regulation of mammalian myosin VI motor function". J. Biol. Chem. 276 (43): 39600–7. doi:10.1074/jbc.M105080200. PMID 11517222.

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