Exploring the role of p97 and its UBX-domain cofactors through identification of their interacting proteins
Research output: Chapter in Book/Report/Conference proceeding › Chapter (peer-reviewed)
|Title of host publication||Ubiquitin family modifiers and the proteasome|
|Subtitle of host publication||reviews and protocols|
|Editors||R. Jürgen Dohmen , Martin Scheffner|
|Number of pages||8|
|Name||Methods in molecular biology|
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.