Integrin Structure, Activation, and Interactions
Top Cited Papers
- 19 January 2011
- journal article
- review article
- Published by Cold Spring Harbor Laboratory in Cold Spring Harbor Perspectives in Biology
- Vol. 3 (3), a004994
- https://doi.org/10.1101/cshperspect.a004994
Abstract
Integrins are large, membrane-spanning, heterodimeric proteins that are essential for a metazoan existence. All members of the integrin family adopt a shape that resembles a large “head” on two “legs,” with the head containing the sites for ligand binding and subunit association. Most of the receptor dimer is extracellular, but both subunits traverse the plasma membrane and terminate in short cytoplasmic domains. These domains initiate the assembly of large signaling complexes and thereby bridge the extracellular matrix to the intracellular cytoskeleton. To allow cells to sample and respond to a dynamic pericellular environment, integrins have evolved a highly responsive receptor activation mechanism that is regulated primarily by changes in tertiary and quaternary structure. This review summarizes recent progress in the structural and molecular functional studies of this important class of adhesion receptor.Keywords
This publication has 89 references indexed in Scilit:
- Structure of an integrin with an αI domain, complement receptor type 4The EMBO Journal, 2009
- The structure of an integrin/talin complex reveals the basis of inside-out signal transductionThe EMBO Journal, 2009
- IntegrinsCell and tissue research, 2009
- The Structure of a Receptor with Two Associating Transmembrane Domains on the Cell Surface: Integrin αIIbβ3Molecular Cell, 2009
- The structure of the integrin αIIbβ3 transmembrane complex explains integrin transmembrane signallingThe EMBO Journal, 2009
- Structure of a Complete Integrin Ectodomain in a Physiologic Resting State and Activation and Deactivation by Applied ForcesMolecular Cell, 2008
- Integrin Conformational Regulation: Uncoupling Extension/Tail Separation from Changes in the Head Region by a Multiresolution ApproachStructure, 2008
- Integrin αIIbβ3 in a Membrane Environment Remains the Same Height after Mn2+ Activation when Observed by Cryoelectron TomographyJournal of Molecular Biology, 2008
- Structure and mechanics of integrin-based cell adhesionCurrent Opinion in Cell Biology, 2007
- Integrins: Bidirectional, Allosteric Signaling MachinesCell, 2002