Scratching the surface: native mass spectrometry of peripheral membrane protein complexes.

Biochemical Society Transactions
Cagla SahinMichael Landreh

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.

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Citations

Nov 10, 2020·Protein Science : a Publication of the Protein Society·Stephen G Sligar, Ilia G Denisov
May 9, 2021·Current Opinion in Structural Biology·Jani R BollaCarol V Robinson
May 27, 2021·Dalton Transactions : an International Journal of Inorganic Chemistry·Jason C CrackNick E Le Brun
Oct 30, 2020·Analytical Chemistry·James E KeenerMichael T Marty
Aug 21, 2021·Chemical Reviews·Sem TamaraAlbert J R Heck
Aug 19, 2021·Chemistry : a European Journal·Julia DornerSimon Drescher

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Methods Mentioned

BETA
X-ray
GTPase
NMR
size exclusion chromatography

Software Mentioned

nMS

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