Identification and mapping of protein-protein interactions by a combination of cross-linking, cleavage, and proteomics

Michael A. Trakselis, Stephen C. Alley, Faoud T. Ishmael

Research output: Contribution to journalReview articlepeer-review

94 Scopus citations

Abstract

Protein-protein interactions are vital for almost all cellular functions, and many require the formation of multiprotein complexes. Identification of the macroscopic and microscopic protein interactions within these complexes is essential in understanding their mechanisms, both under physiologic as well as pathologic conditions. This review describes the current technology available to investigate interactions between proteins utilizing chemical cross-linking and site-directed cleavage reagents, outlining the necessary steps involved in identifying interacting proteins both in vitro and in vivo. Once interacting proteins are identified, more information about the architecture of the assemblies is necessary. Unique separation techniques coupled with cross-linking and mass spectrometry can now identify specific interaction sites and lead to the development of quaternary structural protein models. Furthermore, combination of these methods with proteomic approaches enables the identification and analysis of complex interactions in vivo. Finally, future directions in cross-linking methodologies are discussed.

Original languageEnglish (US)
Pages (from-to)741-750
Number of pages10
JournalBioconjugate Chemistry
Volume16
Issue number4
DOIs
StatePublished - Jul 1 2005

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering
  • Pharmacology
  • Pharmaceutical Science
  • Organic Chemistry

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