Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
Actinin alpha 1
Introduction
Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.[1]
Function
Function
Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This gene encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene.[2]
References
References
- ↑ Youssoufian H, McAfee M, Kwiatkowski DJ (Jul 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”.
- ↑ 3.0 3.1 Dhavan R, Greer PL, Morabito MA, Orlando LR, Tsai LH (September 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. PMID 12223541.
- ↑ Gonzalez AM, Otey C, Edlund M, Jones JC (December 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 (April 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. doi:10.1091/mbc.10.4.819. PMC 25204. PMID 10198040.
- ↑ Vallenius T, Luukko K, Mäkelä TP (April 2000). “CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4”. J. Biol. Chem. 275 (15): 11100–5. doi:10.1074/jbc.275.15.11100. PMID 10753915.
- ↑ Bauer K, Kratzer M, Otte M, de Quintana KL, Hagmann J, Arnold GJ, Eckerskorn C, Lottspeich F, Siess W (December 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 (January 2002). “Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex”. Biochemistry. 41 (4): 1100–8. doi:10.1021/bi0156005. PMID 11802708.
- ↑ Asada M, Irie K, Morimoto K, Yamada A, Ikeda W, Takeuchi M, Takai Y (February 2003). “ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions”. J. Biol. Chem. 278 (6): 4103–11. doi:10.1074/jbc.M209832200. PMID 12446711.
- ↑ Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B (May 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. doi:10.1074/jbc.274.19.13410. PMID 10224105.
- ↑ Li B, Trueb B (September 2001). “Analysis of the alpha-actinin/zyxin interaction”. J. Biol. Chem. 276 (36): 33328–35. doi:10.1074/jbc.M100789200. PMID 11423549.
- ↑ 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. doi:10.1016/j.brainres.2006.07.122. PMID 16973135.
Further reading
Further reading
- Snásel J, Pichová I (1997). “The cleavage of host cell proteins by HIV-1 protease”. Folia Biol. (Praha). 42 (5): 227–30. doi:10.1007/BF02818986. PMID 8997639.
- 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. doi:10.1111/j.1749-6632.1998.tb09629.x. PMID 9599291.
- 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. doi:10.1016/0014-4827(91)90418-T. PMID 1720388.
- 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. doi:10.1016/0014-5793(91)80116-K. PMID 1991513.
- 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. doi:10.1093/nar/17.16.6725. PMCÂ 318366. PMIDÂ 2780298.
- 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. doi:10.1016/0014-5793(95)00362-D. PMID 7750553.
- 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. doi:10.1083/jcb.130.1.67. PMC 2120515. PMID 7790378.
- 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- 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. doi:10.1006/bbrc.1996.1082. PMID 8713105.
- Mukai H, Toshimori M, Shibata H, et al. (1997). “Interaction of PKN with alpha-actinin”. J. Biol. Chem. 272 (8): 4740–6. doi:10.1074/jbc.272.8.4740. PMID 9030526.
- 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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- 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. doi:10.1074/jbc.273.15.9078. PMID 9535896.
- 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. doi:10.1091/mbc.10.4.819. PMC 25204. PMID 10198040.
- 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. doi:10.1074/jbc.274.19.13410. PMID 10224105.
External links
External links
- Actinin, alpha 1 Info with links in the Cell Migration Gateway
- Human ACTN1 genome location and ACTN1 gene details page in the UCSC Genome Browser.