Actinin, alpha 2

Actinin, alpha 2
	; PDB rendering based on 1h8b.
Available structures
PDB	1H8B, 1HCI, 1QUU
Identifiers
Symbols	ACTN2; CMD1AA
External IDs	OMIM: 102573 MGI: 109192 HomoloGene: 31016 GeneCards: ACTN2 Gene
Gene Ontology
Molecular function	• actin binding; • integrin binding; • calcium ion binding; • protein binding; • structural constituent of muscle; • titin binding; • titin binding; • identical protein binding; • ion channel binding; • protein dimerization activity; • ZASP binding; • FATZ 1 binding; • titin Z domain binding;
Cellular component	• extracellular region; • cytoplasm; • cytosol; • cytoskeleton; • actin filament; • focal adhesion; • Z disc; • filopodium; • cortical actin cytoskeleton; • platelet alpha granule lumen; • pseudopodium; • dendritic spine;
Biological process	• platelet degranulation; • cell adhesion; • synaptic transmission; • blood coagulation; • microspike assembly; • muscle filament sliding; • platelet activation; • regulation of apoptotic process; • focal adhesion assembly; • protein homotetramerization;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

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Actinin, alpha 2, also known as ACTN2, is a protein which in humans is encoded by the ACTN2 gene.^[1]

[edit] 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. Studies have also implicated alpha actinin in the binding of cardiac ion channels, K_v1.5 in particular.^[2] This gene encodes a muscle-specific, alpha actinin isoform that is expressed in both skeletal and cardiac muscles. Transcript variants resulting from the use of multiple poly_A sites have been observed.^[1]

[edit] Interactions

Actinin, alpha 2 has been shown to interact with KCNA5,^[2]^[3] DLG1,^[2] DISC1,^[4] MYOZ1,^[5] GRIN2B,^[6] ADAM12,^[7] ACTN3^[8] and MYPN.^[9]

[edit] References

^ ^a ^b "Entrez Gene: ACTN2 actinin, alpha 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=88.
^ ^a ^b ^c Eldstrom, Jodene; Choi Woo Sung, Steele David F, Fedida David (Jul. 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Lett. (Netherlands) 547 (1-3): 205–11. doi:10.1016/S0014-5793(03)00668-9. ISSN 0014-5793. PMID 12860415.
^ Maruoka, N D; Steele D F, Au B P, Dan P, Zhang X, Moore E D, Fedida D (May. 2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Lett. (NETHERLANDS) 473 (2): 188–94. doi:10.1016/S0014-5793(00)01521-0. ISSN 0014-5793. PMID 10812072.
^ Morris, Jill A; Kandpal Geeta, Ma Lei, Austin Christopher P (Jul. 2003). "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation". Hum. Mol. Genet. (England) 12 (13): 1591–608. doi:10.1093/hmg/ddg162. ISSN 0964-6906. PMID 12812986.
^ Faulkner, G; Pallavicini A, Comelli A, Salamon M, Bortoletto G, Ievolella C, Trevisan S, Kojic' S, Dalla Vecchia F, Laveder P, Valle G, Lanfranchi G (Dec. 2000). "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle". J. Biol. Chem. (UNITED STATES) 275 (52): 41234–42. doi:10.1074/jbc.M007493200. ISSN 0021-9258. PMID 10984498.
^ Wyszynski, M; Lin J, Rao A, Nigh E, Beggs A H, Craig A M, Sheng M (Jan. 1997). "Competitive binding of alpha-actinin and calmodulin to the NMDA receptor". Nature (ENGLAND) 385 (6615): 439–42. doi:10.1038/385439a0. ISSN 0028-0836. PMID 9009191.
^ Galliano, M F; Huet C, Frygelius J, Polgren A, Wewer U M, Engvall E (May. 2000). "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion". J. Biol. Chem. (UNITED STATES) 275 (18): 13933–9. doi:10.1074/jbc.275.18.13933. ISSN 0021-9258. PMID 10788519.
^ Chan, Y; Tong H Q, Beggs A H, Kunkel L M (Jul. 1998). "Human skeletal muscle-specific alpha-actinin-2 and -3 isoforms form homodimers and heterodimers in vitro and in vivo". Biochem. Biophys. Res. Commun. (UNITED STATES) 248 (1): 134–9. doi:10.1006/bbrc.1998.8920. ISSN 0006-291X. PMID 9675099.
^ Bang, M L; Mudry R E, McElhinny A S, Trombitás K, Geach A J, Yamasaki R, Sorimachi H, Granzier H, Gregorio C C, Labeit S (Apr. 2001). "Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies". J. Cell Biol. (United States) 153 (2): 413–27. doi:10.1083/jcb.153.2.413. ISSN 0021-9525. PMC 2169455. PMID 11309420. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2169455.

[edit] Further reading

Faulkner G, Lanfranchi G, Valle G (2002). "Telethonin and other new proteins of the Z-disc of skeletal muscle.". IUBMB Life 51 (5): 275–82. doi:10.1080/152165401317190761. PMID 11699871.
Beggs AH, Byers TJ, Knoll JH, et al. (1992). "Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11.". J. Biol. Chem. 267 (13): 9281–8. PMID 1339456.
Beggs AH, Phillips HA, Kozman H, et al. (1992). "A (CA)n repeat polymorphism for the human skeletal muscle alpha-actinin gene ACTN2 and its localization on the linkage map of chromosome 1.". Genomics 13 (4): 1314–5. doi:10.1016/0888-7543(92)90054-V. PMID 1505962.
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.
Pavalko FM, LaRoche SM (1993). "Activation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actinin.". J. Immunol. 151 (7): 3795–807. PMID 8104223.
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.
Wyszynski M, Lin J, Rao A, et al. (1997). "Competitive binding of alpha-actinin and calmodulin to the NMDA receptor.". Nature 385 (6615): 439–42. doi:10.1038/385439a0. PMID 9009191.
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.
Young P, Ferguson C, Bañuelos S, Gautel M (1998). "Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin.". EMBO J. 17 (6): 1614–24. doi:10.1093/emboj/17.6.1614. PMC 1170509. PMID 9501083. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170509.
Zhang S, Ehlers MD, Bernhardt JP, et al. (1998). "Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors.". Neuron 21 (2): 443–53. doi:10.1016/S0896-6273(00)80553-X. PMID 9728925.
Krupp JJ, Vissel B, Thomas CG, et al. (1999). "Interactions of calmodulin and alpha-actinin with the NR1 subunit modulate Ca2+-dependent inactivation of NMDA receptors.". J. Neurosci. 19 (4): 1165–78. PMID 9952395.
Zhou Q, Ruiz-Lozano P, Martone ME, Chen J (1999). "Cypher, a striated muscle-restricted PDZ and LIM domain-containing protein, binds to alpha-actinin-2 and protein kinase C.". J. Biol. Chem. 274 (28): 19807–13. doi:10.1074/jbc.274.28.19807. PMID 10391924.
Faulkner G, Pallavicini A, Formentin E, et al. (1999). "ZASP: a new Z-band alternatively spliced PDZ-motif protein.". J. Cell Biol. 146 (2): 465–75. doi:10.1083/jcb.146.2.465. PMID 10427098.
Tiso N, Majetti M, Stanchi F, et al. (1999). "Fine mapping and genomic structure of ACTN2, the human gene coding for the sarcomeric isoform of alpha-actinin-2, expressed in skeletal and cardiac muscle.". Biochem. Biophys. Res. Commun. 265 (1): 256–9. doi:10.1006/bbrc.1999.1661. PMID 10548523.
Nikolopoulos SN, Spengler BA, Kisselbach K, et al. (2000). "The human non-muscle alpha-actinin protein encoded by the ACTN4 gene suppresses tumorigenicity of human neuroblastoma cells.". Oncogene 19 (3): 380–6. doi:10.1038/sj.onc.1203310. PMID 10656685.
Galliano MF, Huet C, Frygelius J, et al. (2000). "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion.". J. Biol. Chem. 275 (18): 13933–9. doi:10.1074/jbc.275.18.13933. PMID 10788519.
Maruoka ND, Steele DF, Au BP, et al. (2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells.". FEBS Lett. 473 (2): 188–94. doi:10.1016/S0014-5793(00)01521-0. PMID 10812072.
Kotaka M, Kostin S, Ngai S, et al. (2000). "Interaction of hCLIM1, an enigma family protein, with alpha-actinin 2.". J. Cell. Biochem. 78 (4): 558–65. doi:10.1002/1097-4644(20000915)78:4<558::AID-JCB5>3.0.CO;2-I. PMID 10861853.
Parast MM, Otey CA (2000). "Characterization of palladin, a novel protein localized to stress fibers and cell adhesions.". J. Cell Biol. 150 (3): 643–56. doi:10.1083/jcb.150.3.643. PMC 2175193. PMID 10931874. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2175193.
Faulkner G, Pallavicini A, Comelli A, et al. (2001). "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle.". J. Biol. Chem. 275 (52): 41234–42. doi:10.1074/jbc.M007493200. PMID 10984498.

[edit] External links

GeneReviews/NIH/NCBI/UW entry on Familial Hypertrophic Cardiomyopathy Overview

This article on a gene on chromosome 1 is a stub. You can help Wikipedia by expanding it.

[entrez-0] "Entrez Gene: ACTN2 actinin, alpha 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=88.

[pmid12860415-1] Eldstrom, Jodene; Choi Woo Sung, Steele David F, Fedida David (Jul. 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Lett. (Netherlands) 547 (1-3): 205–11. doi:10.1016/S0014-5793(03)00668-9. ISSN 0014-5793. PMID 12860415.

[pmid10812072-2] Maruoka, N D; Steele D F, Au B P, Dan P, Zhang X, Moore E D, Fedida D (May. 2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Lett. (NETHERLANDS) 473 (2): 188–94. doi:10.1016/S0014-5793(00)01521-0. ISSN 0014-5793. PMID 10812072.

[pmid12812986-3] Morris, Jill A; Kandpal Geeta, Ma Lei, Austin Christopher P (Jul. 2003). "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation". Hum. Mol. Genet. (England) 12 (13): 1591–608. doi:10.1093/hmg/ddg162. ISSN 0964-6906. PMID 12812986.

[pmid10984498-4] Faulkner, G; Pallavicini A, Comelli A, Salamon M, Bortoletto G, Ievolella C, Trevisan S, Kojic' S, Dalla Vecchia F, Laveder P, Valle G, Lanfranchi G (Dec. 2000). "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle". J. Biol. Chem. (UNITED STATES) 275 (52): 41234–42. doi:10.1074/jbc.M007493200. ISSN 0021-9258. PMID 10984498.

[pmid9009191-5] Wyszynski, M; Lin J, Rao A, Nigh E, Beggs A H, Craig A M, Sheng M (Jan. 1997). "Competitive binding of alpha-actinin and calmodulin to the NMDA receptor". Nature (ENGLAND) 385 (6615): 439–42. doi:10.1038/385439a0. ISSN 0028-0836. PMID 9009191.

[pmid10788519-6] Galliano, M F; Huet C, Frygelius J, Polgren A, Wewer U M, Engvall E (May. 2000). "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion". J. Biol. Chem. (UNITED STATES) 275 (18): 13933–9. doi:10.1074/jbc.275.18.13933. ISSN 0021-9258. PMID 10788519.

[pmid9675099-7] Chan, Y; Tong H Q, Beggs A H, Kunkel L M (Jul. 1998). "Human skeletal muscle-specific alpha-actinin-2 and -3 isoforms form homodimers and heterodimers in vitro and in vivo". Biochem. Biophys. Res. Commun. (UNITED STATES) 248 (1): 134–9. doi:10.1006/bbrc.1998.8920. ISSN 0006-291X. PMID 9675099.

[pmid11309420-8] Bang, M L; Mudry R E, McElhinny A S, Trombitás K, Geach A J, Yamasaki R, Sorimachi H, Granzier H, Gregorio C C, Labeit S (Apr. 2001). "Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies". J. Cell Biol. (United States) 153 (2): 413–27. doi:10.1083/jcb.153.2.413. ISSN 0021-9525. PMC 2169455. PMID 11309420. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2169455.

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Actinin, alpha 2

Contents

[edit] Function

[edit] Interactions

[edit] References

[edit] Further reading

[edit] External links

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