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LYP inhibits T-cell activation when dissociated from CSK

Lymphoid tyrosine phosphatase ( LYP ) and C-terminal Src kinase ( CSK ) are negative regulators of signaling mediated through the T-cell antigen receptor (TCR) and are thought to act in a cooperative manner when forming a complex. Here we studied the spatiotemporal dynamics of the LYP – CSK complex in T cells. We demonstrate that dissociation of this complex is necessary for recruitment of LYP to the plasma membrane, where it downmodulates TCR signaling. Development of a potent and selective chemical probe of LYP confirmed that LYP inhibits T-cell activation when removed from CSK . Our findings may explain the reduced TCR-mediated signaling associated with a single-nucleotide polymorphism that confers increased risk for certain autoimmune diseases, including type 1 diabetes and rheumatoid arthritis, and results in expression of a mutant LYP that is unable to bind CSK . Our compound also represents a starting point for the development of a LYP -based treatment of autoimmunity. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Chemical Biology Nature Publishing Group (NPG)

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