Approaches for assessing and discovering protein interactions in cancer.
Significant insight into the function of proteins can be delineated by discovering and characterizing interacting proteins. There are numerous methods for the discovery of unknown associated protein networks, with purification of the bait (the protein of interest) followed by mass spectrometry as a common theme. In recent years, advances have permitted the purification of endogenous proteins and methods for scaling down starting material. As such, approaches for rapid, unbiased identification of protein interactomes are becoming a standard tool in the researchers toolbox, rather than a technique that is only available to specialists. This review will highlight some of the recent technical advances in proteomic-based discovery approaches, the pros and cons of various methods and some of the key findings in cancer-related systems.
University of Cambridge, Robinson Way, Cambridge CB2 0RE, United Kingdom. Jason.carroll@cruk.cam.ac.uk.
Hisham
H
Mohammed
Jason S
JS
Carroll
D000818:Animals; D001665:Binding Sites; D006801:Humans; D047468:Immunoprecipitation; D013058:Mass Spectrometry; D009369:Neoplasms / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000302:isolation & purification* / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*
D011506:Proteins