Abstract
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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Acknowledgments
This work was supported by a Grant-in-Aid for Scientific Research on Innovative Areas (Brain Environment; 24111506) from the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan to N.S.
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Shimokawa, N., Koibuchi, N. (2015). Downregulation of Receptor Tyrosine Kinases Through Ubiquitination: Analysis by Immunodetection. In: Germano, S. (eds) Receptor Tyrosine Kinases. Methods in Molecular Biology, vol 1233. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-1789-1_12
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DOI: https://doi.org/10.1007/978-1-4939-1789-1_12
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Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-1788-4
Online ISBN: 978-1-4939-1789-1
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