Integrin Superfamily

Integrins are a superfamily of cell-surface adhesion molecules formed from eight different chains and 18 different chains that assemble as heterodimers to mediate cell–cell and cell–matrix interactions. As sensors of the microenvironment, they control vital cellular functions such as cell growth, differentiation, programmed death, and motility; developmental processes; and in the adult they mediate tissue maintenance, blood clotting and immunity.

Keywords: integrin; cell adhesion; cell trafficking; ligand; extracellular matrix

Figure 1. Structural features of integrins. Schematic illustrations of the structural features of (a) non-I-domain and (b) I-domain integrins. Both I-domain -subunits, and N-terminal regions of -subunits contain a metal ion-dependent adhesion site (MIDAS) motif involved in ligand-binding. -propeller repeats 5–7 of I-domain -subunits, and repeats 4–7 of non-I-domain -subunits contain EF-hand-like cation-binding sequences that bind Ca2+ and negatively regulate ligand-binding. A -turn in the third -propeller repeat involved in ligand-binding by -subunits is denoted by an asterisk. Integrin -subunits contain four repeats of an eight cysteine motif resembling EGF-like motifs that are similar to those of the distant protein relative TIED.
Figure 2. Integrin subunit pairings. There are 18 and 8 integrin subunits from which 24 different functional integrins are currently known to be formed.
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 References
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 Further Reading
    Arnaout MA, Goodman SL and Xiong JP (2002) Coming to grips with integrin binding to ligands. Current Opinion in Cell Biology 14: 641–651.
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Krissansen, Geoffrey W, and Danen, Erik HJ(Apr 2007) Integrin Superfamily. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0000927.pub2]