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- W4281569235 endingPage "1751" @default.
- W4281569235 startingPage "1751" @default.
- W4281569235 abstract "Integrin LFA1 is a cell adhesion receptor expressed exclusively in leukocytes, and plays crucial roles in lymphocyte trafficking, antigen recognition, and effector functions. Since the discovery that the adhesiveness of LFA1 can be dynamically changed upon stimulation, one challenge has been understanding how integrins are regulated by inside-out signaling coupled with macromolecular conformational changes, as well as ligand bindings that transduce signals from the extracellular domain to the cytoplasm in outside-in signaling. The small GTPase Rap1 and integrin adaptor proteins talin1 and kindlin-3 have been recognized as critical molecules for integrin activation. However, their cooperative regulation of integrin adhesiveness in lymphocytes requires further research. Recent advances in single-molecule imaging techniques have revealed dynamic molecular processes in real-time and provided insight into integrin activation in cellular environments. This review summarizes integrin regulation and discusses new findings regarding the bidirectionality of LFA1 activation and signaling processes in lymphocytes." @default.
- W4281569235 created "2022-05-27" @default.
- W4281569235 creator A5020249052 @default.
- W4281569235 creator A5023661305 @default.
- W4281569235 creator A5038256820 @default.
- W4281569235 date "2022-05-26" @default.
- W4281569235 modified "2023-09-25" @default.
- W4281569235 title "LFA1 Activation: Insights from a Single-Molecule Approach" @default.
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