integrin-alpha

^[1]^[2]^[3]^[4]

Function

composed of alpha & beta subunits selected from 16 alpha & 8 beta subunits that heterodimerize to produce more than 20 different receptors^[3]
the short cytoplasmic domains of the alpha & beta subunits do not have intrinsic enzyme activity, but appear to function by nucleating large complexes of cytoskeletal proteins & cytoskeletal-associated protein kinases
integrin beta-4 is the exception, with a cytoplasmic domain in excess of 1000 residues
integrin-alpha(s) contain highly divergent amino acid sequences, whereas the integrin-beta subunits show partial sequence conservation
the integrin-beta(s) target integrins to focal adhesions in a ligand-independent manner, whereas the integrin-alpha(s) regulate the specificity of ligand-dependent interactions

↑ Molecular Cell Biology (2nd ed) Darnell J; Lodish H & Baltimore D (eds), Scientific American Books, WH Freeman, NY 1990, pg 921
↑ Burns K et al Modulation of gene expression by calreticulin binding to glucocorticoid receptor. Nature 367:476 1994 PMID: https://www.ncbi.nlm.nih.gov/pubmed/8107808 {KXGFFKR}
↑ ^3.0 ^3.1 Dedhar et al Inhibition of nuclear hormone receptor activity by calreticulin. Nature 367:480 1994 PMID: https://www.ncbi.nlm.nih.gov/pubmed/8107809 {KXGFFKR}
↑ Clark EA & Brugge JS Integrins and signal transduction pathways: the road taken. Science 268:233 1995 PMID: https://www.ncbi.nlm.nih.gov/pubmed/7716514