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ENABLE SIGNED

Elucidating natural bilayer lipid environments

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EC-Contrib. €

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Project "ENABLE" data sheet

The following table provides information about the project.

Coordinator
THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD 

Organization address
address: WELLINGTON SQUARE UNIVERSITY OFFICES
city: OXFORD
postcode: OX1 2JD
website: www.ox.ac.uk

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Total cost 2˙481˙744 €
 EC max contribution 2˙481˙744 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2015-AdG
 Funding Scheme ERC-ADG
 Starting year 2016
 Duration (year-month-day) from 2016-06-01   to  2021-05-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD UK (OXFORD) coordinator 2˙481˙744.00

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 Project objective

Excising a membrane protein from its natural environment, preserving the lipid bilayer, and characterising the lipids that surround it is the ‘holy grail’ of membrane protein biophysics. However, with some 40,000 different lipid structures the challenges we face in understanding selective binding arise not just from the complexity and dynamics of the lipidome, but also from the transient nature of protein lipid interactions. To overcome these challenges we will take mass spectrometry (MS) into a new era, allowing, for the first time, the study of proteins in an environment as close as possible to the natural one. To do this we will (i) characterise protein lipid interactions by employing a high resolution Orbitrap mass spectrometer developed in-house, specifically for membrane proteins, (ii) capture the native lipid environment in vehicles suitable for use in conjunction with MS, and (iii) establish a new platform to be known as integral membrane protein desorption electrospray ionization (impDESI). Designed and built in-house impDESI is capable of releasing membrane proteins from surfaces directly into the mass spectrometer (MS). We will develop impDESI for membrane mimetics, and subsequently portions of natural membranes, enabling us to extract proteins with oligomeric state preserved and native lipid binding intact. The development of impDESI, in conjunction with high resolution Orbitrap MS, and coupled with the optimisation of membrane mimetics, has the potential to radically transform our understanding of native lipid binding, not only directly, but also temporally and spatially. Together these advances will answer key questions about how lipids modulate protein interfaces, occupy different binding sites, modulate membrane protein structure and modify function in vivo. Given the importance of membrane proteins as potential drugs targets understanding their modulation by lipids would be a major step towards more effective drug development.

 Publications

year authors and title journal last update
List of publications.
2017 Hsin-Yung Yen, Jonathan T. S. Hopper, Idlir Liko, Timothy M. Allison, Ya Zhu, Dejian Wang, Monika Stegmann, Shabaz Mohammed, Beili Wu, Carol V. Robinson
Ligand binding to a G protein–coupled receptor captured in a mass spectrometer
published pages: e1701016, ISSN: 2375-2548, DOI: 10.1126/sciadv.1701016
Science Advances 3/6 2019-02-28
2018 Hsin-Yung Yen, Kin Kuan Hoi, Idlir Liko, George Hedger, Michael R. Horrell, Wanling Song, Di Wu, Philipp Heine, Tony Warne, Yang Lee, Byron Carpenter, Andreas Plückthun, Christopher G. Tate, Mark S. P. Sansom, Carol V. Robinson
PtdIns(4,5)P2 stabilizes active states of GPCRs and enhances selectivity of G-protein coupling
published pages: 423-427, ISSN: 0028-0836, DOI: 10.1038/s41586-018-0325-6
Nature 559/7714 2019-02-28
2018 Dror S. Chorev, Lindsay A. Baker, Di Wu, Victoria Beilsten-Edmands, Sarah L. Rouse, Tzviya Zeev-Ben-Mordehai, Chimari Jiko, Firdaus Samsudin, Christoph Gerle, Syma Khalid, Alastair G. Stewart, Stephen J. Matthews, Kay Grünewald, Carol V. Robinson
Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry
published pages: 829-834, ISSN: 0036-8075, DOI: 10.1126/science.aau0976
Science 362/6416 2019-02-28
2017 Michael Landreh, Erik G. Marklund, Povilas Uzdavinys, Matteo T. Degiacomi, Mathieu Coincon, Joseph Gault, Kallol Gupta, Idlir Liko, Justin L. P. Benesch, David Drew, Carol V. Robinson
Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters
published pages: 13993, ISSN: 2041-1723, DOI: 10.1038/ncomms13993
Nature Communications 8 2019-02-28
2017 Stephen Ambrose, Nicholas G. Housden, Kallol Gupta, Jieyuan Fan, Paul White, Hsin-Yung Yen, Julien Marcoux, Colin Kleanthous, Jonathan T. S. Hopper, Carol V. Robinson
Native Desorption Electrospray Ionization Liberates Soluble and Membrane Protein Complexes from Surfaces
published pages: 14463-14468, ISSN: 1433-7851, DOI: 10.1002/anie.201704849
Angewandte Chemie International Edition 56/46 2019-02-28
2018 Kallol Gupta, Jingwen Li, Idlir Liko, Joseph Gault, Cherine Bechara, Di Wu, Jonathan T S Hopper, Kevin Giles, Justin L P Benesch, Carol V Robinson
Identifying key membrane protein lipid interactions using mass spectrometry
published pages: 1106-1120, ISSN: 1754-2189, DOI: 10.1038/nprot.2018.014
Nature Protocols 13/5 2019-02-28

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