Unit

UNIT 5.28 Identifying Novel Protein-Protein Interactions Using Co-Immunoprecipitation and Mass Spectroscopy

  1. R. Benjamin Free,
  2. Lisa A. Hazelwood,
  3. David R. Sibley

Published Online: 1 JAN 2009

DOI: 10.1002/0471142301.ns0528s46

Current Protocols in Neuroscience

Current Protocols in Neuroscience

How to Cite

Free, R. B., Hazelwood, L. A. and Sibley, D. R. 2009. Identifying Novel Protein-Protein Interactions Using Co-Immunoprecipitation and Mass Spectroscopy. Current Protocols in Neuroscience. 46:5.28:5.28.1–5.28.14.

Author Information

  1. National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland

Publication History

  1. Published Online: 1 JAN 2009
  2. Published Print: JAN 2009

Abstract

Proteomics has evolved from genomic science due to the convergence of advances in protein chemistry, separations, mass spectroscopy, and peptide and protein databases. Where identifying protein-protein interactions was once limited to yeast two-hybrid analyses or empirical data, protein-protein interactions can now be examined in both cells and native tissues by precipitation of the protein complex of interest. Coupling this field to receptor pharmacology has recently allowed for the identification of proteins that differentially and selectively interact with receptors and are integral to their biological effects. It is becoming increasingly apparent that receptors in neurons do not exist as singular independent units, but rather are part of large macromolecular complexes of interacting proteins. It is a primary quest of neuroscience to piece together these interactions and to characterize the regulatory signalplexes of all proteins. This unit presents co-immunoprecipitation-coupled mass spectroscopy as one way of identifying signalplex partners. Curr. Protoc. Neurosci. 46:5.28.1-5.28.14. © 2009 by John Wiley & Sons, Inc.

Keywords:

  • proteomics;
  • neuroreceptors;
  • signalplex;
  • receptor interactions