4.4 Review

Mass spectrometry: a technique of many faces

Journal

QUARTERLY REVIEWS OF BIOPHYSICS
Volume 49, Issue -, Pages -

Publisher

CAMBRIDGE UNIV PRESS
DOI: 10.1017/S0033583516000160

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Funding

  1. European Research Council (ERC) [636752]
  2. Minerva Foundation Grant
  3. Federal Ministry for Education and Research, Germany
  4. Faculty of Life Sciences, Weizmann Institute of Science
  5. Israel Cancer Research Fund
  6. European Research Council (ERC) [636752] Funding Source: European Research Council (ERC)

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Protein complexes form the critical foundation for a wide range of biological process, however understanding the intricate details of their activities is often challenging. In this review we describe how mass spectrometry (MS) plays a key role in the analysis of protein assemblies and the cellular pathways which they are involved in. Specifically, we discuss how the versatility of mass spectrometric approaches provides unprecedented information on multiple levels. We demonstrate this on the ubiquitin-proteasome proteolytic pathway, a process that is responsible for protein turnover. We follow the various steps of this degradation route and illustrate the different MS workflows that were applied for elucidating molecular information. Overall, this review aims to stimulate the integrated use of multiple mass spectrometry approaches for analyzing complex biological systems.

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