Abstract
Integrin receptors connect the extracellular matrix to the actin cytoskeleton. This interaction can be viewed as a cyclical liaison, which develops again and again at new adhesion sites only to cease at sites of de-adhesion. Recent work has demonstrated that multidomain proteins play crucial roles in the integrin-actin connection by providing a high degree of regulation adjusted to the needs of the cell. In this review we present several examples of this paradigm and with special emphasis on the ILK-PINCH-parvin complex, which amply demonstrates how structural and signalling functions are linked together.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Actinin / metabolism
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Actins / metabolism*
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Adaptor Proteins, Signal Transducing
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Animals
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Carrier Proteins / metabolism
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Cell Adhesion / physiology*
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Cytoskeleton / metabolism
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DNA-Binding Proteins / metabolism
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Extracellular Matrix / metabolism
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Focal Adhesion Protein-Tyrosine Kinases
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Integrins / metabolism*
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Intracellular Signaling Peptides and Proteins*
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Membrane Proteins*
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Microfilament Proteins / metabolism
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Protein Serine-Threonine Kinases / metabolism
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Protein-Tyrosine Kinases / metabolism
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Signal Transduction / physiology*
Substances
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Actins
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Adaptor Proteins, Signal Transducing
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Carrier Proteins
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DNA-Binding Proteins
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ITGB1BP1 protein, human
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Integrins
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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Microfilament Proteins
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PARVA protein, human
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PARVB protein, human
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Actinin
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integrin-linked kinase
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Protein-Tyrosine Kinases
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Focal Adhesion Protein-Tyrosine Kinases
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Protein Serine-Threonine Kinases