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Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton.

Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.

GTPases act as important switches in many signaling events in cells. Although small and heterotrimeric G proteins are subjects of intensive studies, little is known about the large IFN-inducible GTPases. In this article, we show that the IFN-γ-inducible guanylate binding protein 1 (GBP-1) is a regulator of T cell activation. Silencing of GBP-1 leads to enhanced activation of early T cell Ag receptor/CD3 signaling molecules, including Lck, that is translated to higher IL-2 production. Mass spectrometry analyses showed that regulatory cytoskeletal proteins, like plastin-2 that bundles actin fibers and spectrin β-chain, brain 1 that links the plasma membrane to the actin cytoskeleton, are binding partners of GBP-1. The spectrin cytoskeleton influences cell spreading and surface expression of TCR/CD3 and the leukocyte phosphatase CD45. We found higher cell spreading and enhanced surface expression of TCR/CD3 and CD45 in GBP-1 silenced T cells that explain their enhanced TCR/CD3 signaling. We conclude that GBP-1 is a downstream processor of IFN-γ via which T cells regulate cytoskeleton-dependent cell functions.

J. Immunol. 192:771-781(2014) [PubMed] [Europe PMC]

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