Scratching the surface: Native mass spectrometry of peripheral membrane protein complexes

Cagla Sahin, Deseree J. Reid, Michael T. Marty, Michael Landreh

Research output: Contribution to journalReview articlepeer-review

13 Scopus citations

Abstract

A growing number of integral membrane proteins have been shown to tune their activity by selectively interacting with specific lipids. The ability to regulate biological functions via lipid interactions extends to the diverse group of proteins that associate only peripherally with the lipid bilayer. However, the structural basis of these interactions remains challenging to study due to their transient and promiscuous nature. Recently, native mass spectrometry has come into focus as a new tool to investigate lipid interactions in membrane proteins. Here, we outline how the native MS strategies developed for integral membrane proteins can be applied to generate insights into the structure and function of peripheral membrane proteins. Specifically, native MS studies of proteins in complex with detergent-solubilized lipids, bound to lipid nanodiscs, and released from native-like lipid vesicles all shed new light on the role of lipid interactions. The unique ability of native MS to capture and interrogate protein-protein, protein-ligand, and protein-lipid interactions opens exciting new avenues for the study of peripheral membrane protein biology.

Original languageEnglish (US)
Pages (from-to)547-558
Number of pages12
JournalBiochemical Society transactions
Volume48
Issue number2
DOIs
StatePublished - Apr 2020

ASJC Scopus subject areas

  • Biochemistry

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