title: An efficient way of studying protein-protein interactions involving HIF-α, c-Myc, and Sp1.
abstract: Protein-protein interaction is an essential biochemical event that mediates various cellular processes including gene expression, intracellular signaling, and intercellular interaction. Understanding such interaction is key to the elucidation of mechanisms of cellular processes in biology and diseases. The hypoxia-inducible transcription factor HIF-1α possesses a non-transcriptional activity that competes with c-Myc for Sp1 binding, whereas its isoform HIF-2α lacks Sp1-binding activity due to phosphorylation. Here, we describe the use of in vitro translation to effectively investigate the dynamics of protein-protein interactions among HIF-1α, c-Myc, and Sp1 and to demonstrate protein phosphorylation as a molecular determinant that functionally distinguishes HIF-2α from HIF-1α.
authors.affiliation: School of Pharmacy, The Chinese University of Hong Kong, Hong Kong, China.
authors.forename: Kenneth K-W
authors.initials: KK
authors.lastname: To
authors.forename: L Eric
authors.initials: LE
authors.lastname: Huang
mesh_terms: D001667:Binding, Competitive; D051795:Hypoxia-Inducible Factor 1, alpha Subunit / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D016271:Proto-Oncogene Proteins c-myc / Q000378:metabolism*; D016329:Sp1 Transcription Factor / Q000378:metabolism*; D015533:Transcriptional Activation
chemical_list: D051795:Hypoxia-Inducible Factor 1, alpha Subunit; D016271:Proto-Oncogene Proteins c-myc; D016329:Sp1 Transcription Factor