title: Strategies for membrane interaction proteomics: no mass spectrometry required.
abstract: Membrane-bound proteins are one of the most important protein types in the cell, and are involved in many major cell processes and signaling pathways. Most proteins, including those at membranes, must interact with other proteins to form complexes, which are essential for their function(s). In this review, we describe some of the major non-mass spectrometry-based methods and technologies used for the investigation of intracellular membrane protein complexes including Tango, fluorescence/bioluminescence resonance energy transfer (F/BRET), luminescence-based mammalian interactome mapping (LUMIER), protein-fragment complementation assay (PCA), and membrane yeast two-hybrid assay (MYTH). We highlight the advantages and drawbacks of these methods, describe recent studies utilizing these methods, and discuss some of the major findings in the study of membrane protein-based cell pathways.
authors.affiliation: Donnelly Centre for Cellular and Biomolecular Research, Department of Biochemistry and Molecular Genetics, University of Toronto, Toronto, ON, Canada.
authors.forename: Mandy H Y
authors.initials: MH
authors.lastname: Lam
authors.forename: Igor
authors.initials: I
authors.lastname: Stagljar
mesh_terms: D000818:Animals; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction; D020798:Two-Hybrid System Techniques
chemical_list: D008565:Membrane Proteins