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CYLD: deubiquitination-induced TCR signaling

Deubiquitinating enzymes remove polyubiquitin chains from and alter the fate of specific target proteins. The CYLD deubiquitinating enzyme regulates proximal T cell receptor signaling in thymocytes by selectively binding to and deubiquitinating the active form of the kinase Lck.

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Figure 1: After engagement of the TCR by self peptide–MHC complexes, phosphorylated Lck is recruited to the CD3 complex, where it phosphorylates and activates Zap70, which then propagates the signal through adaptor proteins and second messengers.

Katie Ris

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Lineberry, N., Fathman, C. CYLD: deubiquitination-induced TCR signaling. Nat Immunol 7, 369–370 (2006). https://doi.org/10.1038/ni0406-369

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