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]
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- ↑ 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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Bibliografía
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