Actinin, alpha 1

Actinin, alpha 1

PDB rendering based on 1sjj.
Identifiers
Symbols ACTN1; FLJ40884; FLJ54432
External IDs OMIM102575 MGI2137706 HomoloGene55553 GeneCards: ACTN1 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 87 109711
Ensembl ENSG00000072110 ENSMUSG00000015143
UniProt P12814 A1BN54
RefSeq (mRNA) NM_001102.3 NM_134156.2
RefSeq (protein) NP_001093.1 NP_598917.1
Location (UCSC) Chr 14:
69.34 – 69.45 Mb
Chr 12:
81.27 – 81.36 Mb
PubMed search [1] [2]

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 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 nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene.[2]

Contents

Interactions

Actinin, alpha 1 has been shown to interact with PDLIM1,[3][4] Collagen, type XVII, alpha 1,[5] CDK5R1,[6] Zyxin,[7][8] Protein kinase N1,[9] GIPC1,[10] SSX2IP[11] and CDK5R2.[6]

See also

References

  1. ^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1683765. 
  2. ^ "Entrez Gene: ACTN1 actinin, alpha 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=87. 
  3. ^ Vallenius, T; Luukko K, Mäkelä T P (Apr. 2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. (UNITED STATES) 275 (15): 11100–5. doi:10.1074/jbc.275.15.11100. ISSN 0021-9258. PMID 10753915. 
  4. ^ Bauer, K; Kratzer M, Otte M, de Quintana K L, Hagmann J, Arnold G J, Eckerskorn C, Lottspeich F, Siess W (Dec. 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 (UNITED STATES) 96 (13): 4236–45. ISSN 0006-4971. PMID 11110697. 
  5. ^ Gonzalez, A M; Otey C, Edlund M, Jones J C (Dec. 2001). "Interactions of a hemidesmosome component and actinin family members". J. Cell. Sci. (England) 114 (Pt 23): 4197–206. ISSN 0021-9533. PMID 11739652. 
  6. ^ a b Dhavan, Rani; Greer Paul L, Morabito Maria A, Orlando Lianna R, Tsai Li-Huei (Sep. 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. (United States) 22 (18): 7879–91. PMID 12223541. 
  7. ^ 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. (UNITED STATES) 274 (19): 13410–8. doi:10.1074/jbc.274.19.13410. ISSN 0021-9258. PMID 10224105. 
  8. ^ Li, B; Trueb B (Sep. 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. (United States) 276 (36): 33328–35. doi:10.1074/jbc.M100789200. ISSN 0021-9258. PMID 11423549. 
  9. ^ Feng, Shuju; Reséndiz Julio C, Christodoulides Nicolaos, Lu Xin, Arboleda David, Berndt Michael C, Kroll Michael H (Jan. 2002). "Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex". Biochemistry (United States) 41 (4): 1100–8. doi:10.1021/bi0156005. ISSN 0006-2960. PMID 11802708. 
  10. ^ Bunn, R C; Jensen M A, Reed B C (Apr. 1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell (UNITED STATES) 10 (4): 819–32. ISSN 1059-1524. PMC 25204. PMID 10198040. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=25204. 
  11. ^ Asada, Masanori; Irie Kenji, Morimoto Koji, Yamada Akio, Ikeda Wataru, Takeuchi Masakazu, Takai Yoshimi (Feb. 2003). "ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions". J. Biol. Chem. (United States) 278 (6): 4103–11. doi:10.1074/jbc.M209832200. ISSN 0021-9258. PMID 12446711. 

Further reading

External links