Paxillin

Paxillin
Rendering based on PDB 1KKY.
Available structures PDB 1KKY, 1KL0, 2O9V, 2VZD, 2VZG, 2VZI, 3GM1
Identifiers
Symbols	PXN; FLJ16691
External IDs	OMIM: 602505 MGI: 108295 HomoloGene: 37697 GeneCards: PXN Gene
Gene Ontology Molecular function • protein binding • beta-catenin binding • zinc ion binding • vinculin binding • metal ion binding Cellular component • cytoplasm • cytoskeleton • microtubule associated complex • plasma membrane • plasma membrane • plasma membrane • focal adhesion • lamellipodium • cell junction Biological process • muscle contraction • cell adhesion • cell-matrix adhesion • signal transduction • signal complex assembly • epidermal growth factor receptor signaling pathway • cell junction assembly • cellular response to reactive oxygen species • growth hormone receptor signaling pathway Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5829	19303
Ensembl	ENSG00000089159	ENSMUSG00000029528
UniProt	P49023	O88294
RefSeq (mRNA)	NM_001080855.1	NM_011223
RefSeq (protein)	NP_001074324.1	NP_035353
Location (UCSC)	Chr 12: 120.65 – 120.7 Mb	Chr 5: 115.96 – 116.01 Mb
PubMed search	[1]	[2]

Paxillin is a signal transduction adaptor protein discovered in 1990 in the laboratory of Keith Burridge and should not be confused with the neurotoxin paxilline. The C-terminal region of paxillin contains four LIM domains that target paxillin to focal adhesions, it is presumed through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal region of paxillin is rich in protein–protein interaction sites. The proteins that bind to paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization, such as COOL/PIX and PKL/GIT. Paxillin is tyrosine-phosphorylated by FAK and Src upon integrin engagement or growth factor stimulation, creating binding sites for the adapter protein Crk.

Further reading

• Turner CE (1998). "Paxillin.". Int. J. Biochem. Cell Biol. 30 (9): 955–59. doi:10.1016/S1357-2725(98)00062-4. PMID 9785458. 
• Panetti TS (2002). "Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration.". Front. Biosci. 7: d143–50. doi:10.2741/panetti. PMID 11779709. 
• Rose DM, Han J, Ginsberg MH (2003). "Alpha4 integrins and the immune response.". Immunol. Rev. 186: 118–24. doi:10.1034/j.1600-065X.2002.18611.x. PMID 12234367. 
• Salgia R, Uemura N, Okuda K et al (1996). "CRKL links p210BCR/ABL with paxillin in chronic myelogenous leukemia cells". J. Biol. Chem. 270 (49): 29145–50. doi:10.1074/jbc.270.49.29145. PMID 7493940. 
• Turner CE, Miller JT (1994). "Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region". J. Cell. Sci. 107 (6): 1583–91. PMID 7525621. 
• Bergman M, Joukov V, Virtanen I, Alitalo K (1995). "Overexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreading". Mol. Cell. Biol. 15 (2): 711–22. PMC 231937. PMID 7529872. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231937. 
• Salgia R, Li JL, Lo SH et al (1995). "Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL". J. Biol. Chem. 270 (10): 5039–47. doi:10.1074/jbc.270.10.5039. PMID 7534286. 
• Schaller MD, Otey CA, Hildebrand JD, Parsons JT (1995). "Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains". J. Cell Biol. 130 (5): 1181–7. doi:10.1083/jcb.130.5.1181. PMC 2120552. PMID 7657702. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120552. 
• Yoshida M, Westlin WF, Wang N et al (1996). "Leukocyte adhesion to vascular endothelium induces E-selectin linkage to the actin cytoskeleton". J. Cell Biol. 133 (2): 445–55. doi:10.1083/jcb.133.2.445. PMC 2120789. PMID 8609175. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120789. 
• Salgia R, Sattler M, Pisick E et al (1996). "p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120c-Cbl". Exp. Hematol. 24 (2): 310–3. PMID 8641358. 
• Salgia R, Pisick E, Sattler M et al (1996). "p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene". J. Biol. Chem. 271 (41): 25198–203. doi:10.1074/jbc.271.41.25198. PMID 8810278. 
• Brown MC, Perrotta JA, Turner CE (1997). "Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding". J. Cell Biol. 135 (4): 1109–23. doi:10.1083/jcb.135.4.1109. PMC 2133378. PMID 8922390. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133378. 
• Retta SF, Barry ST, Critchley DR et al (1997). "Focal adhesion and stress fiber formation is regulated by tyrosine phosphatase activity". Exp. Cell Res. 229 (2): 307–17. doi:10.1006/excr.1996.0376. PMID 8986614. 
• Mazaki Y, Hashimoto S, Sabe H (1997). "Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins". J. Biol. Chem. 272 (11): 7437–44. doi:10.1074/jbc.272.11.7437. PMID 9054445. 
• Hiregowdara D, Avraham H, Fu Y et al (1997). "Tyrosine phosphorylation of the related adhesion focal tyrosine kinase in megakaryocytes upon stem cell factor and phorbol myristate acetate stimulation and its association with paxillin". J. Biol. Chem. 272 (16): 10804–10. doi:10.1074/jbc.272.16.10804. PMID 9099734. 
• Ostergaard HL, Lou O, Arendt CW, Berg NN (1998). "Paxillin phosphorylation and association with Lck and Pyk2 in anti-CD3- or anti-CD45-stimulated T cells". J. Biol. Chem. 273 (10): 5692–6. doi:10.1074/jbc.273.10.5692. PMID 9488700. 
• Fernandez R, Suchard SJ (1998). "Syk activation is required for spreading and H2O2 release in adherent human neutrophils". J. Immunol. 160 (10): 5154–62. PMID 9590268. 
• Lewis JM, Schwartz MA (1998). "Integrins regulate the association and phosphorylation of paxillin by c-Abl". J. Biol. Chem. 273 (23): 14225–30. doi:10.1074/jbc.273.23.14225. PMID 9603926. 
• Ganju RK, Munshi N, Nair BC et al (1998). "Human Immunodeficiency Virus Tat Modulates the Flk-1/KDR Receptor, Mitogen-Activated Protein Kinases, and Components of Focal Adhesion in Kaposi's Sarcoma Cells". J. Virol. 72 (7): 6131–7. PMC 110419. PMID 9621077. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110419. 
• Deakin NO, Turner CE (2008). "Paxillin comes of age". J. Cell. Sci. 121 (Pt 15): 2435–44. doi:10.1242/jcs.018044. PMC 2522309. PMID 18650496. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2522309. 

External links

• MBInfo: Paxillin
• Paxillin Info with links in the Cell Migration Gateway
• MeSH Paxillin