Actinin, alpha 2

From Wikipedia, the free encyclopedia

Actinin, alpha 2

PDB rendering based on 1h8b.

Available structures: 1h8b, 1hci, 1quu, 1tjt, 1wku

Identifiers

Symbol(s)

ACTN2;

External IDs

OMIM: 102573 MGI: 109192 HomoloGene: 31016

Gene ontology
Molecular Function:	• actin binding • integrin binding • calcium ion binding • structural constituent of muscle • thyroid hormone receptor coactivator activity • protein homodimerization activity • ZASP binding • FATZ 1 binding
Cellular Component:	• cytoskeleton • actin filament • focal adhesion • Z disc • filopodium • pseudopodium • dendritic spine
Biological Process:	• muscle contraction • cell adhesion • microspike biogenesis • regulation of apoptosis • focal adhesion formation • protein homotetramerization

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001103 (mRNA)
NP_001094 (protein)

NM_033268 (mRNA)
NP_150371 (protein)

Location

Chr 1: 234.92 - 234.99 Mb

Chr 13: 12.32 - 12.4 Mb

Pubmed search

[1]

[2]

Actinin, alpha 2, also known as ACTN2, is a human gene.^[1]

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 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] References

^ ^a ^b Entrez Gene: ACTN2 actinin, alpha 2.

[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. 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. 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 ( Pt 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. PMID 8609175.
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. 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. PMID 9501083.
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. 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. 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. 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. 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. 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. 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. PMID 10931874.
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.