IndraLab

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OTUD7B leads to the ubiquitination of ZAP70. 4 / 4
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"For example, Otud7b-mediated ZAP70 deubiquitination inhibits the association of ZAP70 with a negative-regulatory phosphatase, Sts1 or Sts2, thereby promoting TCR/CD28-stimulated ZAP70 phosphorylation [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Importantly, the Otud7b deficiency substantially enhanced the ubiquitination of Zap70 (XREF_FIG), and the Otud7b knockdown in EL4 cells also enhanced the TCR-CD28-stimulated Zap70 ubiquitination (XREF_FIG)."
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"We further demonstrated that by deubiquitinating Zap70, Otud7b prevented the association of Zap70 with the phosphatase Sts1/2, thereby facilitating Zap70 phosphorylation and TCR signaling."
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"This possibility is further suggested by our present finding that Otud7b deficiency promotes Zap70 ubiquitination and inhibits Zap70 phosphorylation in both CD4 + and CD8 + T cells."
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