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Molecular mechanisms of leukocyte β2 integrin activation. | LitMetric

Molecular mechanisms of leukocyte β2 integrin activation.

Blood

Center for Autoimmunity and Inflammation, La Jolla Institute for Immunology, La Jolla, CA.

Published: June 2022

AI Article Synopsis

Article Abstract

Integrins are transmembrane receptors that mediate cell-cell and cell-extracellular matrix adhesion. Although all integrins can undergo activation (affinity change for ligands), the degree of activation is most spectacular for integrins on blood cells. The β2 integrins are exclusively expressed on the surface of all leukocytes including neutrophils, lymphocytes, and monocytes. They are essential for many leukocyte functions and are strictly required for neutrophil arrest from rolling. The inside-out integrin activation process receives input from chemokine receptors and adhesion molecules. The integrin activation pathway involves many cytoplasmic signaling molecules such as spleen tyrosine kinase, other kinases like Bruton's tyrosine kinase, phosphoinositide 3-kinases, phospholipases, Rap1 GTPases, and the Rap1-GTP-interacting adapter molecule. These signaling events ultimately converge on talin-1 and kindlin-3, which bind to the integrin β cytoplasmic domain and induce integrin conformational changes: extension and high affinity for ligand. Here, we review recent structural and functional insights into how talin-1 and kindlin-3 enable integrin activation, with a focus on the distal signaling components that trigger β2 integrin conformational changes and leukocyte adhesion under flow.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10082358PMC
http://dx.doi.org/10.1182/blood.2021013500DOI Listing

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