Abstract
The elucidation of protein–protein interaction networks can provide preliminary insights into the function of uncharacterized proteins based on the interactions they establish in the cell. Here, we describe a protein immunoprecipitation protocol that can be used in combination with mass spectrometry analysis to identify the p97 interactome as well as specific subgroups of proteins interacting with its UBX-domain adaptors. This approach aims to dissect the role played by individual UBX cofactors within the complex array of cellular functions performed by p97.
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Acknowledgments
This protocol was established while G.A. was a postdoctoral scholar at the California Institute of Technology in Pasadena, CA. We thank Susanne Bandau for critical reading of the manuscript.
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Alexandru, G. (2012). Exploring the Role of p97 and Its UBX-Domain Cofactors Through Identification of Their Interacting Proteins. In: Dohmen, R., Scheffner, M. (eds) Ubiquitin Family Modifiers and the Proteasome. Methods in Molecular Biology, vol 832. Humana Press. https://doi.org/10.1007/978-1-61779-474-2_21
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DOI: https://doi.org/10.1007/978-1-61779-474-2_21
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