Biology:Alpha-actinin-1

From HandWiki
Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.[1]

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-1 is an F-actin cross-linking protein – a bundling protein that is thought to anchor actin to a number of intracellular structures.[2] Alpha-actinin-1 is a non-muscle cytoskeletal isoform 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.[3]

Interactions

Alpha-actinin-1 has been shown to interact with:

See also

References

  1. "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. Jul 1990. PMID 2349951. 
  2. "ACTN2 - Alpha-actinin-2 - Homo sapiens (Human) - ACTN2 gene & protein" (in en). https://www.uniprot.org/uniprot/P35609. 
  3. "Entrez Gene: ACTN1 actinin, alpha 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=87. 
  4. 4.0 4.1 "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. September 2002. doi:10.1523/JNEUROSCI.22-18-07879.2002. PMID 12223541. 
  5. "Interactions of a hemidesmosome component and actinin family members". J. Cell Sci. 114 (Pt 23): 4197–206. December 2001. doi:10.1242/jcs.114.23.4197. PMID 11739652. https://cdr.lib.unc.edu/downloads/d217qz52s. 
  6. "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. April 1999. doi:10.1091/mbc.10.4.819. PMID 10198040. 
  7. "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. 275 (15): 11100–5. April 2000. doi:10.1074/jbc.275.15.11100. PMID 10753915. 
  8. "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. December 2000. doi:10.1182/blood.V96.13.4236. PMID 11110697. 
  9. "Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex". Biochemistry 41 (4): 1100–8. January 2002. doi:10.1021/bi0156005. PMID 11802708. 
  10. "ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions". J. Biol. Chem. 278 (6): 4103–11. February 2003. doi:10.1074/jbc.M209832200. PMID 12446711. 
  11. "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol. Chem. 274 (19): 13410–8. May 1999. doi:10.1074/jbc.274.19.13410. PMID 10224105. 
  12. "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. September 2001. doi:10.1074/jbc.M100789200. PMID 11423549. 
  13. "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT).". Brain Res 1116 (1): 50–7. 2006. doi:10.1016/j.brainres.2006.07.122. PMID 16973135. https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=16973135. 

Further reading

External links