Actinin

Actinin is a microfilament protein. The functional protein is an anti-parallel dimer, which cross-links the thin filaments in adjacent sarcomeres, and therefore coordinates contractions between sarcomeres in the horizontal axis. Alpha-actinin is a part of the spectrin superfamily. This superfamily is made of spectrin, dystrophin, and their homologous and isoforms. In non-muscle cells, it is found by the actin filaments and at the adhesion sites[1].The lattice like arrangement provides stability to the muscle contractile apparatus.[1] Specifically, it helps bind actin filaments to the cell membrane.[2] There is a binding site at each end of the rod and with bundles of actin filaments.[1]

The non-sarcomeric alpha-actinins, encoded by ACTN1 and ACTN4, are widely expressed. ACTN2 expression is found in both cardiac and skeletal muscle, whereas ACTN3 is limited to the latter. Both ends of the rod-shaped alpha-actinin dimer contain actin-binding domains. Six different proteins are produced from four alpha-actinin encoding genes.These six proteins can further be divided into two different groups: muscle (calcium insensitive) and non-muscle cytoskeletal (calcium sensitive) isoforms.[1]

  1. ^ a b c d Sjöblom B, Salmazo A, Djinović-Carugo K (September 2008). "Alpha-actinin structure and regulation". Cellular and Molecular Life Sciences. 65 (17): 2688–2701. doi:10.1007/s00018-008-8080-8. PMC 11131806. PMID 18488141. S2CID 26321210.
  2. ^ Broderick MJ, Winder SJ (January 2005). "Spectrin, alpha-actinin, and dystrophin". Advances in Protein Chemistry. Fibrous Proteins: Coiled-Coils, Collagen and Elastomers. 70. Academic Press: 203–246. doi:10.1016/S0065-3233(05)70007-3. ISBN 9780120342709. PMID 15837517. Retrieved 2023-11-06.