integrin
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Function
- cell surface receptors
- interact with the extracellular matrix
- role in attachment to other cells
- mediate intracellular signals
- role in cell shape, mobility, cell cycle
- bidirectional signalling[5]
- extracellular to intracellular signalling
- intracellular to extracellular signalling
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
- CD49 or Very Late Antigen (VLA)
- glycoprotein IIB/IIIA
- integrin alpha-10/beta-1
- integrin alpha-11/beta-1
- integrin alpha-2b/beta-3
- integrin alpha-4/beta-7
- integrin alpha-6/beta-4
- integrin alpha-7/beta-1
- integrin alpha-8/beta-1
- integrin alpha-9/beta-1
- integrin alpha-D/beta-2 (CD11d/CD18)
- integrin alpha-E/beta-7
- integrin alpha-M/beta-2 (CD11b/CD18, MAC1)
- integrin alpha-V/beta-3
- integrin alpha-V/beta-5
- integrin alpha-V/beta-6
- integrin alpha-V/beta-8
- integrin alpha-X/beta-2 (CD11c/CD18)
- lymphocyte function-associated antigen-1 (LFA-1, leukocyte adhesion protein LFA-1, integrin alpha-L/beta-2, CD11a/CD18)
- vitronectin receptor
References
- ↑ Springer TA. Adhesion receptors of the immune system. Nature. 1990 Aug 2;346(6283):425-34. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/1974032
- ↑ Molecular Cell Biology (2nd ed) Darnell J; Lodish H & Baltimore D (eds), Scientific American Books, WH Freeman, NY 1990, pg 921
- ↑ 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
- ↑ Humphries MJf Integrin structure Biochem Soc Trans 2000, 28:311 PMID: https://www.ncbi.nlm.nih.gov/pubmed/10961914
- ↑ 5.0 5.1 Hynes R Integrins: bidirectional, allosteric signaling machines Cell 2002, 110:683 PMID: https://www.ncbi.nlm.nih.gov/pubmed/12297042
- ↑ Wikipedia; Note: Integrin entry http://en.wikipedia.org/wiki/integrin