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Alfa-actinina-1
A alfa-actinina-1 (nome de UniProt[1]), é unha proteína que nos humanos está codificada no xene ACTN1 do cromosoma 14.[2]
Función
As alfa-actininas pertencen á superfamilia de xenes da espectrina, que son un grupo diverso de proteínas citoesqueléticas, que inclúen as alfa e beta espectrinas e as distrofinas. A alfa-actinina-1 é unha proteína que establece enlaces cruzados coa F-actina. É unha proteína que intervén na formación de feixes de actina e pénsase que ancora a actina a diversas estruturas intracelulares.[1] A alfa-actinina-1 é unha isoforma citoesquelética non muscular que se encontra ao longo de feixes de microfilamentos e unións de tipo adherente, onde está implicada na unión da actina ás membranas. En contraste, as isoformas esqueléticas, cardíacas e do músculo liso están localizadas no disco Z e corpos densos análogos, onde axudan ancorar os filamentos de actina miofibrilar.[3]
Interaccións
A alfa-actinina-1 presenta interaccións con:
Notas
- ↑ 1,0 1,1 "ACTN2 - Alpha-actinin-2 - Homo sapiens (Human) - ACTN2 gene & protein". www.uniprot.org (en inglés). Consultado o 5 de decembro de 2021.
- ↑ Youssoufian H, McAfee M, Kwiatkowski DJ (xullo de 1990). "Cloning and chromosomal localization of the human cytoskeletal alpha-actinin gene reveals linkage to the beta-spectrin gene". Am J Hum Genet 47 (1): 62–72. PMC 1683765. PMID 2349951.
- ↑ "Entrez Gene: ACTN1 actinin, alpha 1".
- ↑ 4,0 4,1 Dhavan R, Greer PL, Morabito MA, Orlando LR, Tsai LH (setembro de 2002). "The cyclin-dependent kinase 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent manner". J. Neurosci. 22 (18): 7879–91. PMC 6758084. PMID 12223541. doi:10.1523/JNEUROSCI.22-18-07879.2002.
- ↑ Gonzalez AM, Otey C, Edlund M, Jones JC (decembro de 2001). "Interactions of a hemidesmosome component and actinin family members". J. Cell Sci. 114 (Pt 23): 4197–206. PMID 11739652.
- ↑ Bunn RC, Jensen MA, Reed BC (abril de 1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell 10 (4): 819–32. PMC 25204. PMID 10198040. doi:10.1091/mbc.10.4.819.
- ↑ Vallenius T, Luukko K, Mäkelä TP (abril de 2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. 275 (15): 11100–5. PMID 10753915. doi:10.1074/jbc.275.15.11100.
- ↑ Bauer K, Kratzer M, Otte M, de Quintana KL, Hagmann J, Arnold GJ, Eckerskorn C, Lottspeich F, Siess W (decembro de 2000). "Human CLP36, a PDZ-domain and LIM-domain protein, binds to alpha-actinin-1 and associates with actin filaments and stress fibers in activated platelets and endothelial cells". Blood 96 (13): 4236–45. PMID 11110697.
- ↑ Feng S, Reséndiz JC, Christodoulides N, Lu X, Arboleda D, Berndt MC, Kroll MH (xaneiro de 2002). "Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex". Biochemistry 41 (4): 1100–8. PMID 11802708. doi:10.1021/bi0156005.
- ↑ Asada M, Irie K, Morimoto K, Yamada A, Ikeda W, Takeuchi M, Takai Y (febreiro de 2003). "ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions". J. Biol. Chem. 278 (6): 4103–11. PMID 12446711. doi:10.1074/jbc.M209832200.
- ↑ Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B (maio de 1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol. Chem. 274 (19): 13410–8. PMID 10224105. doi:10.1074/jbc.274.19.13410.
- ↑ Li B, Trueb B (setembro de 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. PMID 11423549. doi:10.1074/jbc.M100789200.
- ↑ Besco JA, Hooft van Huijsduijnen R, Frostholm A, Rotter A (2006). "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT).". Brain Res 1116 (1): 50–7. PMID 16973135. doi:10.1016/j.brainres.2006.07.122.
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Outros artigos
Bibliografía
- Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease.". Folia Biol. (Praha) 42 (5): 227–30. PMID 8997639. doi:10.1007/BF02818986.
- Menko S, Philp N, Veneziale B, Walker J (1998). "Integrins and development: how might these receptors regulate differentiation of the lens.". Ann. N. Y. Acad. Sci. 842: 36–41. PMID 9599291. doi:10.1111/j.1749-6632.1998.tb09629.x.
- Yürüker B, Niggli V (1992). "Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network.". J. Cell Sci. 101 (2): 403–14. PMID 1629252.
- Tokuue Y, Goto S, Imamura M, et al. (1992). "Transfection of chicken skeletal muscle alpha-actinin cDNA into nonmuscle and myogenic cells: dimerization is not essential for alpha-actinin to bind to microfilaments.". Exp. Cell Res. 197 (2): 158–67. PMID 1720388. doi:10.1016/0014-4827(91)90418-T.
- Shoeman RL, Kesselmier C, Mothes E, et al. (1991). "Non-viral cellular substrates for human immunodeficiency virus type 1 protease.". FEBS Lett. 278 (2): 199–203. PMID 1991513. doi:10.1016/0014-5793(91)80116-K.
- Nishiyama M, Ozturk M, Frohlich M, et al. (1990). "Expression of human alpha-actinin in human hepatocellular carcinoma.". Cancer Res. 50 (19): 6291–4. PMID 2169343.
- Millake DB, Blanchard AD, Patel B, Critchley DR (1989). "The cDNA sequence of a human placental alpha-actinin.". Nucleic Acids Res. 17 (16): 6725. PMC 318366. PMID 2780298. doi:10.1093/nar/17.16.6725.
- Dubernard V, Faucher D, Launay JM, Legrand C (1995). "Identification of the cytoskeletal protein alpha-actinin as a platelet thrombospondin-binding protein.". FEBS Lett. 364 (2): 109–14. PMID 7750553. doi:10.1016/0014-5793(95)00362-D.
- Knudsen KA, Soler AP, Johnson KR, Wheelock MJ (1995). "Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin.". J. Cell Biol. 130 (1): 67–77. PMC 2120515. PMID 7790378. doi:10.1083/jcb.130.1.67.
- Glück U, Ben-Ze'ev A (1995). "Modulation of alpha-actinin levels affects cell motility and confers tumorigenicity on 3T3 cells.". J. Cell Sci. 107 (7): 1773–82. PMID 7983147.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. PMID 8125298. doi:10.1016/0378-1119(94)90802-8.
- Egerton M, Moritz RL, Druker B, et al. (1996). "Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes.". Biochem. Biophys. Res. Commun. 224 (3): 666–74. PMID 8713105. doi:10.1006/bbrc.1996.1082.
- Mukai H, Toshimori M, Shibata H, et al. (1997). "Interaction of PKN with alpha-actinin.". J. Biol. Chem. 272 (8): 4740–6. PMID 9030526. doi:10.1074/jbc.272.8.4740.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1–2): 149–56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3.
- Hazan RB, Norton L (1998). "The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton.". J. Biol. Chem. 273 (15): 9078–84. PMID 9535896. doi:10.1074/jbc.273.15.9078.
- Bunn RC, Jensen MA, Reed BC (1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton.". Mol. Biol. Cell 10 (4): 819–32. PMC 25204. PMID 10198040. doi:10.1091/mbc.10.4.819.
- Reinhard M, Zumbrunn J, Jaquemar D, et al. (1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment.". J. Biol. Chem. 274 (19): 13410–8. PMID 10224105. doi:10.1074/jbc.274.19.13410.
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