A paxilina é unha proteína que funciona como proteína adaptadora na transdución de sinais descuberta en 1990, á que se lle deu o nome en inglés de paxillin, do latín paxillus, que significa "pequeno poste"[1] (non confundir co alcaloide neurotóxico chamado en inglés paxilline).[2] A paxilina ten 68 kDa e localízase no citoplasma nos puntos onde a célula se une á matriz extracelular formando adhesións focais.[3] A rexión C-terminal da paxilina contén catro dominios LIM que serven para que a paxilina se una ás adhesións focais. Crese que nas adhesións focais establece unha asociación directa coa cola citoplasmática da beta-integrina. A rexión N-terminal da paxilina é rica en sitios para a interacción proteína-proteína. As proteínas que se unen á paxilina son diversas e entre elas están proteína tirosina quinases, como a Src e a quinase de adhesión focal (FAK), proteínas estruturais, como a vinculina e actopaxina, e reguladores da organización da actina, como COOL/PIX e PKL/GIT. A paxilina é fosforilada na tirosina por FAK e Src despois da súa unión a integrinas ou a estimulación por factores de crecemento, creando sitios de unión para a proteína adaptadora Crk.[4] A paxilina axuda a recrutar moléculas no complexo de transdución de sinais do que forma parte, facilitando a recepción de estímulos externos que modulan diversos procesos celulares, e intervindo así na adhesión celular, mobilidade e crecemento celular.[3]
![](//upload.wikimedia.org/wikipedia/commons/thumb/e/e3/Protein_PXN_PDB_1KKY.png/220px-Protein_PXN_PDB_1KKY.png) |
PDB 1KKY |
Paxilina |
Identificadores |
Símbolo |
PXN |
Símbolos alt. |
FLJ16691 |
Entrez |
5829 |
OMIM |
602505 |
PDB |
1KL0, 1OW6, 1OW7, 1OW8, 2K2R, 2O9V, 2VZD, 2VZG, 2VZI, 3GM1, 3PY7, 3RQE, 3RQF, 3RQG, 3U3C, 3U3F, 4EDN 1KKY, 1KL0, 1OW6, 1OW7, 1OW8, 2K2R, 2O9V, 2VZD, 2VZG, 2VZI, 3GM1, 3PY7, 3RQE, 3RQF, 3RQG, 3U3C, 3U3F, 4EDN |
RefSeq |
NP_001074324 |
UniProt |
P49023 |
Outros datos |
Locus |
Cr. 12 120.65 – 120.7 Mb |
Turner, C. E., Glenney, J. R., Jr. & Burridge, K. Paxillin: a new vinculin-binding protein present in focal adhesions. J Cell Biol 111, 1059–1068 (1990).
Bibliografía
- Panetti TS (2002). "Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration.". Front. Biosci. 7: d143–50. PMID 11779709. doi:10.2741/panetti.
- Rose DM, Han J, Ginsberg MH (2003). "Alpha4 integrins and the immune response.". Immunol. Rev. 186: 118–24. PMID 12234367. doi:10.1034/j.1600-065X.2002.18611.x.
- 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. PMID 7493940. doi:10.1074/jbc.270.49.29145.
- 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.
- 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. PMID 7534286. doi:10.1074/jbc.270.10.5039.
- 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. PMC 2120552. PMID 7657702. doi:10.1083/jcb.130.5.1181.
- 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. PMC 2120789. PMID 8609175. doi:10.1083/jcb.133.2.445.
- 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. PMID 8810278. doi:10.1074/jbc.271.41.25198.
- 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. PMC 2133378. PMID 8922390. doi:10.1083/jcb.135.4.1109.
- 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. PMID 8986614. doi:10.1006/excr.1996.0376.
- 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. PMID 9054445. doi:10.1074/jbc.272.11.7437.
- 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. PMID 9099734. doi:10.1074/jbc.272.16.10804.
- 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. PMID 9488700. doi:10.1074/jbc.273.10.5692.
- 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. PMID 9603926. doi:10.1074/jbc.273.23.14225.
- 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.
- Deakin NO, Turner CE (2008). "Paxillin comes of age". J. Cell. Sci. 121 (Pt 15): 2435–44. PMC 2522309. PMID 18650496. doi:10.1242/jcs.018044.