Publications in Scientific Journals:

F. Forster, W. Paster, V. Supper, P. Schatzlmaier, S. Sunzenauer, N. Ostler, A. Saliba, P. Eckerstorfer, N. Britzen-Laurent, G. Schütz, J. Schmid, G. Zlabinger, E. Naschberger, M. Stürzl, H. Stockinger:
"Guanylate Binding Protein 1-Mediated Interaction of T Cell Antigen Receptor Signaling with the Cytoskeleton";
Journal of Immunology, 192 (2014), 771 - 781.

English abstract:
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-g-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 b-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-g via which T cells regulate cytoskeleton-dependent cell functions.

Created from the Publication Database of the Vienna University of Technology.