title: Proteomic approaches to the analysis of multiprotein signaling complexes.
abstract: Signal transduction is one of the most active fields in modern biomedical research. Increasing evidence has shown that signaling proteins associate with each other in characteristic ways to form large signaling complexes. These diverse structures operate to boost signaling efficiency, ensure specificity and increase sensitivity of the biochemical circuitry. Traditional methods of protein analysis are inadequate to fully characterize and understand these structures, which are intricate, contain many components and are highly dynamic. Instead, proteomics technologies are currently being applied to investigate the nature and composition of multimeric signaling complexes. This review presents commonly used and potential proteomic methods of analyzing diverse protein complexes along with a discussion and a brief evaluation of alternative approaches. Challenges associated with proteomic analysis of signaling complexes are also discussed.
authors.affiliation: The Urological Diseases Research Center, Department of Urology, Children's Hospital Boston, Boston, MA 02115, USA.
authors.forename: Wei
authors.initials: W
authors.lastname: Yang
authors.forename: Hanno
authors.initials: H
authors.lastname: Steen
authors.forename: Michael R
authors.initials: MR
authors.lastname: Freeman
mesh_terms: D000345:Affinity Labels; D018604:Epitope Mapping; D047468:Immunoprecipitation; D007553:Isotope Labeling; D013058:Mass Spectrometry; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000302:isolation & purification / Q000502:physiology*; D010750:Phosphoproteins / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction / Q000502:physiology*; D054928:Validation Studies as Topic
chemical_list: D000345:Affinity Labels; D046912:Multiprotein Complexes; D010750:Phosphoproteins