title: Integrin avidity regulation: are changes in affinity and conformation underemphasized?
abstract: 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.
mesh_terms: 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
chemical_list: 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