The covalent attachment of ubiquitin to a protein is one of the most common post-translational modifications and regulates diverse eukaryotic cellular processes. Ubiquitination of MHC class I was fi rst described in the context of viral proteins which target MHC class I for degradation in the endoplasmic reticulum and at the cell surface. Study of viral-induced MHC class I degradation has been extremely instructive in elucidating cellular pathways for degradation of membrane and secretory proteins. More recently, ubiquitination of endogenous MHC class I heavy chains which fail to achieve their native conformation and undergo endoplasmic-reticulum associated degradation has been demonstrated. In this chapter we describe methods for identification of endogenous ubiquitinated MHC class I heavy chains by MHC class I-immunoprecipitation and ubiquitin-specific immunoblot or by metabolic labeling and immunoprecipitation. © Springer Science+Business Media, LLC 2013.
CITATION STYLE
Burr, M. L., Boname, J. M., & Lehner, P. J. (2013). Studying ubiquitination of mhc class i molecules. Methods in Molecular Biology, 960, 109–125. https://doi.org/10.1007/978-1-62703-218-6_9
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