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- W1981591257 abstract "Lsc is a hematopoietic-restricted protein that functions as an effector of G alpha(12/13)-associated G-protein coupled receptors that activates RhoA. In the absence of Lsc leukocytes exhibit impaired migration and B lymphocytes inefficiently resolve integrin-mediated adhesion. Here, we demonstrate that Lsc exists physiologically in primary B lymphocytes as a large molecular weight complex resembling a homo-tetramer. Interfering with the assembly of this large molecular weight Lsc oligomer results in the activation of both Lsc functional activities and leads to cell rounding and inhibition of integrin-mediated adhesion. During cell migration on integrin ligands we find Lsc localizes predominantly toward the rear of migrating cells where we suggest it activates RhoA to resolve integin-mediated adhesion. Together these data demonstrate that Lsc regulates integrin-mediated adhesive events at the trailing edge of migrating cells." @default.
- W1981591257 created "2016-06-24" @default.
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- W1981591257 date "2008-04-01" @default.
- W1981591257 modified "2023-09-27" @default.
- W1981591257 title "Lsc activity is controlled by oligomerization and regulates integrin adhesion" @default.
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- W1981591257 doi "https://doi.org/10.1016/j.molimm.2007.11.002" @default.
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