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Statements

EGF phosphorylates USP8. 5 / 5
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"2 and 3 suggest that the mechanism responsible for EGF-induced Usp8 tyrosine phosphorylation might be the same for EGFR and ErbB2."
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"In EGFR-ErbB2 expressing cells, EGF-induced Usp8 tyrosine phosphorylation was even lower in the presence of PD153035 than the Usp8 tyrosine phosphorylation level observed in unstimulated and mock-trea[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"As we have demonstrated before, deletion of the MIT-domain in Usp8 results in decreased EGF-induced Usp8 tyrosine phosphorylation [17] ."
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"Collectively, these data demonstrate that the Cbl binding site of the wild-type EGFR and the EGFR-ErbB2 chimera is not required for efficient EGF-induced Usp8 tyrosine phosphorylation or coprecipitati[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In cells expressing either EGFR ( Fig. 6 A and C ) or EGFR-ErbB2 ( Fig. 6 B and D), removal of the MIT domain (Usp8 Δ140) resulted in a decrease of the EGF-induced Usp8 tyrosine phosphorylation, when [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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