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Phosphorylation of oncogenic MET receptor tyrosine kinase can be positively regulated by PD‐L1 through inhibiting PTP1B. Silencing of PD‐L1 led to increased PTP1B protein levels, possibly through suppressing its degradation, which in turn resulted in increased dephosphorylation of MET and its downstream kinase ERKs, and reduced cell proliferation. PD‐L1 induction by IFN‐γ promoted MET phosphorylation, possibly associated with suppression of PTP1B
