After ligand binding, receptor tyrosine kinases (RTKs) transmit intracellular signals involved in the regulation of various cell events and then attenuate signal transduction. Ubiquitination is a critical step involved in the downregulation of RTK signaling. Here, we describe how to immunodetect the ligand-induced ubiquitination and degradation of TrkA, an RTK, by immunoprecipitation and Western blotting.
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