IndraLab

Statements

ZAP70 binds OTUD7B. 11 / 11
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sparser
"Domain mapping analyses revealed the requirement of the N-terminal UBA domain of Otud7b for its physical interaction with Zap70 ( xref ), indicating the facilitation of Otud7b–Zap70 interaction by ubiquitination."
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"Otud7b binds to and deubiquitinates Zap70."
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sparser
"In response to TCR signaling, Otud7b was rapidly recruited to Zap70 via a mechanism that required the UBA domain of Otud7b, suggesting the possibility that Otud7b interacted with ubiquitinated Zap70."
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sparser
"Interestingly, although Otud7b did not bind Zap70 in resting T cells, these two proteins formed a complex upon TCR–CD28 stimulation ( xref )."
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"Upon TCR stimulation, OTUD7B binds to and deubiquitinates Zap70, thereby preventing the binding of Sts1 and 2 [ xref ]."
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reach
"Otud7b binds to and deubiquitinates Zap70, thereby preventing the interaction of Zap70 with the negative-regulatory phosphatases, Sts1 and Sts2 199 (XREF_FIG)."
27012466
sparser
"In response to TCR–CD28 ligation, Otud7b rapidly bound to Zap70 and inhibited Zap70 ubiquitination."
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"In response to TCR-CD28 ligation, Otud7b rapidly bound to Zap70 and inhibited Zap70 ubiquitination."
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"This ubiquitination-defective Zap70 mutant was also attenuated in association with Otud7b, consistent with the idea that the Zap70–Otud7b interaction might be facilitated by Zap70 ubiquitination ( xref )."
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"The Otud7b–Zap70 interaction was further confirmed using a transient transfection experiment in which the overexpressed Otud7b strongly associated with Zap70 ( xref )."
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"The Otud7b-Zap70 interaction was further confirmed using a transient transfection experiment in which the overexpressed Otud7b strongly associated with Zap70 (XREF_FIG)."
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