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Bach, T.L. et al.

PI3K regulates pleckstrin-2 in T-cell cytoskeletal reorganization.

Pleckstrin-2 is composed of 2 pleckstrin homology (PH) domains and a disheveled-Egl-10-pleckstrin (DEP) domain. A lipid-binding assay revealed that pleckstrin-2 binds with greatest affinity to D3 and D5 phosphoinositides. Pleckstrin-2 expressed in Jurkat T cells bound to the cellular membrane and enhanced actin-dependent spreading only after stimulation of the T-cell antigen receptor or the integrin alpha4beta1. A pleckstrin-2 variant containing point mutations in both PH domains failed to associate with the Jurkat membrane and had no effect on spreading under the same conditions. Although still membrane bound, a pleckstrin-2 variant containing point mutations in the DEP domain demonstrated a decreased ability to induce membrane ruffles and spread. Pleckstrin-2 also colocalized with actin at the immune synapse and integrin clusters via its PH domains. Although pleckstrin-2 can bind to purified D3 and D5 phosphoinositides, the intracellular membrane association of pleckstrin-2 and cell spreading are dependent on D3 phosphoinositides, because these effects were disrupted by pharmacologic inhibition of phosphatidylinositol 3-kinase ( PI3K). Our results indicate that pleckstrin-2 uses its modular domains to bind to membrane- associated phosphatidylinositols generated by PI3K, whereby it coordinates with the actin cytoskeleton in lymphocyte spreading and immune synapse formation.[1]

References

PI3K regulates pleckstrin-2 in T-cell cytoskeletal reorganization. Bach, T.L., Kerr, W.T., Wang, Y., Bauman, E.M., Kine, P., Whiteman, E.L., Morgan, R.S., Williamson, E.K., Ostap, E.M., Burkhardt, J.K., Koretzky, G.A., Birnbaum, M.J., Abrams, C.S. Blood (2007) [Pubmed]

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