Exploring the role of p97 and its UBX-domain cofactors through identification of their interacting proteins
Research output: Chapter in Book/Report/Conference proceeding › Other chapter contribution
| Original language | English |
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| Title | Methods in Molecular Biology |
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| Subtitle | Ubiquitin Family Modifiers and the Proteasome |
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| Publisher | Springer |
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| Publication date | 1-Jan-2012 |
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| Pages | 305-312 |
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| Number of pages | 8 |
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| Volume | 832 |
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| ISBN (Print) | 9781617794735 |
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| DOIs | |
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| State | Published |
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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. © 2012 Springer Science+Business Media, LLC.