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- W2097736544 abstract "The protein phosphatase LYP is known to regulate signaling in the immune system, but the regulatory mechanisms controlling LYP itself are less clear. Exploration of spatiotemporal dynamics and application of a newly identified chemical inhibitor now define a role for the kinase CSK in dialing down LYP activity. 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." @default.
- W2097736544 created "2016-06-24" @default.
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- W2097736544 date "2012-03-18" @default.
- W2097736544 modified "2023-10-17" @default.
- W2097736544 title "LYP inhibits T-cell activation when dissociated from CSK" @default.
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- W2097736544 doi "https://doi.org/10.1038/nchembio.916" @default.
- W2097736544 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3329573" @default.
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