integrin-beta
Jump to navigation
Jump to search
Function
- regulatory subunit of integrins
- target integrins to focal adhesions (ligand-dependent)
Structure
- 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
More general terms
More specific terms
- CD104 (integrin-beta 4, GP150, ITGB4)
- CD18 (integrin beta-2, L-CAM beta, ITGB2, CD18, MFI7)
- CD29; integrin-beta 1; fibronectin receptor beta; platelet glycoprotein IIa; VLA-4 beta (ITGB1, FNRB, MDF2, MSK12)
- CD61 (integrin-beta 3, platelet membrane glycoprotein IIIA, GPIIIA, ITGB3, GP3A)
- integrin-beta 5 (ITGB5)
- integrin-beta 6 (ITGB6)
- integrin-beta 7 (ITGB7)
- integrin-beta 8 (ITGB8)
Component of
References
- ↑ Molecular Cell Biology (2nd ed) Darnell J; Lodish H & Baltimore D (eds), Scientific American Books, WH Freeman, NY 1990, pg 921
- ↑ Stossel TP. On the crawling of animal cells. Science. 1993 May 21;260(5111):1086-94. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/8493552
- ↑ 3.0 3.1 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