Mass spectrometry accelerates membrane protein analysis

Jeffrey N. Savas, Benjamin D. Stein, Christine C. Wu, John R. Yates*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

78 Scopus citations

Abstract

Cellular membranes are composed of proteins and glyco- and phospholipids and play an indispensible role in maintaining cellular integrity and homeostasis, by physically restricting biochemical processes within cells and providing protection. Membrane proteins perform many essential functions, which include operating as transporters, adhesion-anchors, receptors, and enzymes. Recent advancements in proteomic mass spectrometry have resulted in substantial progress towards the determination of the plasma membrane (PM) proteome, resolution of membrane protein topology, establishment of numerous receptor protein complexes, identification of ligand-receptor pairs, and the elucidation of signaling networks originating at the PM. Here, we discuss the recent accelerated success of discovery-based proteomic pipelines for the establishment of a complete membrane proteome.

Original languageEnglish (US)
Pages (from-to)388-396
Number of pages9
JournalTrends in Biochemical Sciences
Volume36
Issue number7
DOIs
StatePublished - Jul 2011

Funding

We would like to thank Guoan Zhang, Thomas Neubert, Joris de Wit and Terunaga Nakagawa for useful discussions regarding the determination of signaling networks, and membrane protein interactions. Additionally, Albert Heck provided critical reading of the review, and Emily J. Larrimer gave valuable editorial advice. Many of the ideas presented here were developed through scientific discussion with current members of the Yates Laboratory. The authors would like to acknowledge funding support from NIH grants P41 RR011823 and 5R01 MH067880 to JY.

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry

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