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LCP1 preferentially binds clasped αMβ2 integrin and attenuates leukocyte adhesion under flow.

Tseng HY, Samarelli AV, Kammerer P, Scholze S, Ziegler T, Immler R, Zent R, Sperandio M, Sanders CR, Fässler R, Böttcher RT
J Cell Sci. 2018 131 (22)

PMID: 30333137 · PMCID: PMC6262777 · DOI:10.1242/jcs.218214

Integrins are α/β heterodimers that interconvert between inactive and active states. In the active state the α/β cytoplasmic domains recruit integrin-activating proteins and separate the transmembrane and cytoplasmic (TMcyto) domains (unclasped TMcyto). Conversely, in the inactive state the α/β TMcyto domains bind integrin-inactivating proteins, resulting in the association of the TMcyto domains (clasped TMcyto). Here, we report the isolation of integrin cytoplasmic tail interactors using either lipid bicelle-incorporated integrin TMcyto domains (α5, αM, αIIb, β1, β2 and β3 integrin TMcyto) or a clasped, lipid bicelle-incorporated αMβ2 TMcyto. Among the proteins found to preferentially bind clasped rather than the isolated αM and β2 subunits was L-plastin (LCP1, also known as plastin-2), which binds to and maintains the inactive state of αMβ2 integrin and thereby regulates leukocyte adhesion to integrin ligands under flow. Our findings offer a global view on cytoplasmic proteins interacting with different integrins and provide evidence for the existence of conformation-specific integrin interactors.

© 2018. Published by The Company of Biologists Ltd.

MeSH Terms (14)

Animals Cell Adhesion Cell Membrane Cytoplasm HEK293 Cells Humans Leukocytes Macrophage-1 Antigen Mice Mice, Inbred C57BL Microfilament Proteins Protein Binding Protein Conformation RAW 264.7 Cells

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