IndraLab

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OTUD7B leads to the dephosphorylation of ZAP70. 5 / 5
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"Because Otud7b deficiency attenuated Zap70 phosphorylation without affecting activation of its upstream kinase Lck, we hypothesized that the enhanced Zap70 ubiquitination in Otud7b -/- T cells might promote the recruitment of a negative regulator to reduce the phosphorylation of Zap70."
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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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"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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"Otud7b deficiency inhibited TCR-CD28-stimulated phosphorylation of Zap70, Akt, and Erks in both naive CD4 + T cells (XREF_FIG) and naive CD8 + T cells (XREF_FIG)."
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"As seen in primary T cells, Otud7b knockdown by shRNA profoundly inhibited the TCR-CD28-stimulated phosphorylation of Zap70, as well as several downstream kinases (XREF_FIG)."
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