Methods for the study of protein-protein interactions in cancer cell biology.
Development of sensitive methods to monitor and quantitatively assess the expression levels of endogenous genes and the association-interaction of proteins in living cells and whole organisms is a complex and challenging problem. In this chapter, we have described basic methods for investigating protein-protein interactions which include immunoprecipitation, GST pull-down assays, peptide bead pull-down assays, chemical crosslinking and photoaffinity labeling. These methods should provide important tools to dissect crosstalk between proteins and the direct implications of this crosstalk in signaling pathways and cancer biology.
Price
Daniel
D
Division of Experimental Medicine, Beth Israel-Deaconess Medical Center and Harvard Medical School, Boston, MA, USA.
Park
Iha
I
Avraham
Hava
H
D002462:Cell Membrane / Q000378:metabolism; D003432:Cross-Linking Reagents; D006801:Humans; D009369:Neoplasms / Q000378:metabolism*; D019920:Photoaffinity Labels; D011233:Precipitin Tests / Q000379:methods*; D011506:Proteins / Q000302:isolation & purification / Q000378:metabolism*; D020239:Receptor Cross-Talk; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism; D015398:Signal Transduction
D003432:Cross-Linking Reagents; D019920:Photoaffinity Labels; D011506:Proteins; D011993:Recombinant Fusion Proteins