Mechanisms that regulate adaptor binding to beta-integrin cytoplasmic tails.
Cells recognize and respond to their extracellular environment through transmembrane receptors such as integrins, which physically connect the extracellular matrix to the cytoskeleton. Integrins provide the basis for the assembly of intracellular signaling platforms that link to the cytoskeleton and influence nearly every aspect of cell physiology; however, integrins possess no enzymatic or actin-binding activity of their own and thus rely on adaptor molecules, which bind to the short cytoplasmic tails of integrins, to mediate and regulate these functions. Many adaptors compete for relatively few binding sites on integrin tails, so regulatory mechanisms have evolved to reversibly control the spatial and temporal binding of specific adaptors. This Commentary discusses the adaptor proteins that bind directly to the tails of beta integrins and, using talin, tensin, filamin, 14-3-3 and integrin-linked kinase (ILK) as examples, describes the ways in which their binding is regulated.
Legate
Kyle R
KR
Department of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany. legate@biochem.mpg.de
Fässler
Reinhard
R
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003593:Cytoplasm / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D006801:Humans; D039641:Integrin beta Chains / Q000378:metabolism*; D008840:Microfilament Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D003598:Cytoskeletal Proteins; D039641:Integrin beta Chains; D008840:Microfilament Proteins