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Mass spectrometry: a technique of many faces

Published online by Cambridge University Press:  28 November 2016

Maya A. Olshina  and
Michal Sharon
Maya A. Olshina
Affiliation:
Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel
Michal Sharon*
Affiliation:
Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel
*
*Author for correspondence: Prof. M. Sharon, Department of Biomolecular Sciences, Weizmann Institute of Science, 234 Herzl St, Rehovot 7610001, Israel. Tel.: +972-8-934-3947; Fax: +972-8-934-6010; Email: [email protected]
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Abstract

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.

Type
Review
Information
Quarterly Reviews of Biophysics , Volume 49 , 2016 , e18
Copyright
Copyright © Cambridge University Press 2016 

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