Structure and mechanics of integrin-based cell adhesion

• Published in: Current opinion in cell biology Vol. 19; no. 5; pp. 495 - 507
• Main Authors: Arnaout, M Amin, Goodman, Simon L, Xiong, Jian-Ping
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.10.2007
• Subjects: Animals; Cell Adhesion - physiology; Crystallography, X-Ray; Cytoskeletal Proteins - chemistry; Cytoskeletal Proteins - metabolism; Focal Adhesions - metabolism; Integrins - chemistry; Integrins - metabolism; Integrins - ultrastructure; Internal Medicine; Ligands; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Subunits - chemistry; Protein Subunits - metabolism; Signal Transduction - physiology; Talin - metabolism
• ISSN: 0955-0674; 1879-0410
• DOI: 10.1016/j.ceb.2007.08.002

Integrins are α/β heterodimeric adhesion glycoprotein receptors that regulate a wide variety of dynamic cellular processes such as cell migration, phagocytosis, and growth and development. X-ray crystallography of the integrin ectodomain revealed its modular architecture and defined its metal-dependent interaction with extracellular ligands. This interaction is regulated from inside the cell (inside-out activation), through the short cytoplasmic α and β integrin tails, which also mediate biochemical and mechanical signals transmitted to the cytoskeleton by the ligand-occupied integrins, effecting major changes in cell shape, behavior, and fate. Recent advances in the structural elucidation of integrins and integrin-binding cytoskeleton proteins are the subjects of this review.