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USP15 leads to the phosphorylation of SMAD1. 3 / 3

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"Herhaus and coworkers showed that USP15 can interact with and deubiquitinate BMP type I receptors, thereby promoting phosphorylation of Smad1 (Herhaus et al., 2014)."

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sparser

"We show that USP15 enhances BMP-induced phosphorylation of SMAD1 by interacting with and deubiquitylating ALK3."

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sparser

"Further characterisation of the role of USP15 in the BMP pathway established that USP15 enhances BMP-induced phosphorylation of SMAD1 and transcription."

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IndraLab

Statements

USP15 leads to the phosphorylation of SMAD1. 3 / 3

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