Based in part on the previous version of this eLS article ‘Integrin Superfamily’ (2007) by Geoffrey W Krissansen and Erik HJ Danen.
Published Online: 20 SEP 2013
Copyright © 2001 John Wiley & Sons, Ltd. All rights reserved.
How to Cite
Danen, E. H. 2013. Integrin Superfamily. eLS. .
- Published Online: 20 SEP 2013
Integrins are cell-surface adhesion molecules formed from eight different β chains and 18 different α chains that assemble as heterodimeric transmembrane receptors to mediate cell–cell and cell–matrix interactions. The integrin superfamily first emerged in the metazoa and has expanded with evolution creating 24 different integrins in humans, each recognising a distinct subset of extracellular ligands. Ligands include extracellular matrix proteins found in basement membranes such as laminins or in fibrilar matrices such as collagen or fibronectin meshworks, as well as counter receptors on neighbouring cells. The adhesive potential of integrins can be regulated and their cytoplasmic tails connect through a dynamic protein interaction network to the cytoskeleton. Thus, integrins provide cells with the capacity to sense and respond to their microenvironment and they control vital cellular functions for embryonic development, tissue homoeostasis, blood clotting and immunity.
Integrins are heterodimeric transmembrane receptors that mediate cell adhesion to the microenvironment.
More than 600 Mya integrins emerged and the integrin superfamily has expanded throughout evolution.
In humans, 24 different integrins are formed from 18 α and 8 β subunits.
Integrins recognise a wide range of ligands, including extracellular matrix proteins, counter receptors on neighbouring cells, plasma proteins, and microbes and viruses.
Integrins couple the extracellular microenvironment to the cytoskeleton through a protein interaction network associated with their cytoplasmic tails.
- cell adhesion;
- extracellular matrix;
- gene knockout studies