Integrin avidity regulation: are changes in affinity and conformation underemphasized?
Integrins play critical roles in development, wound healing, immunity and cancer. Central to their function is their unique ability to modulate dynamically their adhesiveness through both affinity- and valency-based mechanisms. Recent advances have shed light on the structural basis for affinity regulation and on the signaling mechanisms responsible for both affinity and valency modes of regulation.
D048868:Adaptor Proteins, Signal Transducing; D000818:Animals; D051017:Apoptosis Regulatory Proteins; D001665:Binding Sites; D002448:Cell Adhesion; D002462:Cell Membrane / Q000378:metabolism; D002465:Cell Movement; D016764:Cell Polarity; D006801:Humans; D016023:Integrins / Q000378:metabolism*; D016169:Lymphocyte Function-Associated Antigen-1 / Q000378:metabolism; D008968:Molecular Conformation; D020559:Monomeric GTP-Binding Proteins; D011485:Protein Binding; D017434:Protein Structure, Tertiary / Q000502:physiology; D021122:Protein Subunits / Q000378:metabolism; D015398:Signal Transduction; D016608:Talin / Q000378:metabolism; D020827:rap1 GTP-Binding Proteins / Q000378:metabolism
D048868:Adaptor Proteins, Signal Transducing; D051017:Apoptosis Regulatory Proteins; D016023:Integrins; D016169:Lymphocyte Function-Associated Antigen-1; D021122:Protein Subunits; C454042:RASSF5 protein, human; D016608:Talin; D020559:Monomeric GTP-Binding Proteins; D020827:rap1 GTP-Binding Proteins