title: Exploring the role of p97 and its UBX-domain cofactors through identification of their interacting proteins.
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.
authors.affiliation: Protein Ubiquitylation Unit, The Scottish Institute for Cell Signalling (SCILLS), University of Dundee, Dundee, Scotland, UK. g.alexandru@dundee.ac.uk
authors.forename: Gabriela
authors.initials: G
authors.lastname: Alexandru
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000378:metabolism*; D002460:Cell Line; D057809:HEK293 Cells; D006801:Humans; D047468:Immunoprecipitation / Q000379:methods*; D013058:Mass Spectrometry / Q000379:methods*; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D060066:Protein Interaction Maps; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism; D057149:Ubiquitinated Proteins / Q000737:chemistry / Q000378:metabolism; D000074405:Valosin Containing Protein
chemical_list: D018797:Cell Cycle Proteins; D025801:Ubiquitin; D057149:Ubiquitinated Proteins; D000251:Adenosine Triphosphatases; D000074405:Valosin Containing Protein