The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The role of interfacial lipids in stabilizing membrane protein oligomers
Open accessAbstract
Oligomerization of membrane proteins in response to lipid binding has a critical role in many cell-signalling pathways but is often difficult to define or predict. Here we report the development of a mass spectrometry platform to determine simultaneously the presence of interfacial lipids and oligomeric stability and to uncover how lipids act as key regulators of membrane-protein association. Evaluation of oligomeric strength for a dataset of 125 α-helical oligomeric membrane proteins reveals an absence of interfacial lipids in the mass spectra of 12 membrane proteins with high oligomeric stability. For the bacterial homologue of the eukaryotic biogenic transporters (LeuT, one of the proteins with the lowest oligomeric stability), we found a precise cohort of lipids within the dimer interface. Delipidation, mutation of lipid-binding sites or expression in cardiolipin-deficient Escherichia coli abrogated dimer formation. Molecular dynamics simulation revealed that cardiolipin acts as a bidentate ligand, bridging across subunits. Subsequently, we show that for the Vibrio splendidus sugar transporter SemiSWEET, another protein with low oligomeric stability, cardiolipin shifts the equilibrium from monomer to functional dimer. We hypothesized that lipids are essential for dimerization of the Na+/H+ antiporter NhaA from E. coli, which has the lowest oligomeric strength, but not for the substantially more stable homologous Thermus thermophilus protein NapA. We found that lipid binding is obligatory for dimerization of NhaA, whereas NapA has adapted to form an interface that is stable without lipids. Overall, by correlating interfacial strength with the presence of interfacial lipids, we provide a rationale for understanding the role of lipids in both transient and stable interactions within a range of α-helical membrane proteins, including G-protein-coupled receptors.
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Cites
‘Improved parameters for the Martini coarse-grained protein force field’
de Jong, D. H., Singh, G., Bennett, W. F. D., Arnarez, C., Wassenaar, T. A., Schäfer, L. V., Periole, X., Tieleman, D. P., & Marrink, S. J. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct300646g · Cited by 1,486
Marty, M. T., Baldwin, A. J., Marklund, E. G., Hochberg, G. K. A., Benesch, J. L. P., & Robinson, C. V. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00140 · Cited by 1,000
Self-citationThe Role of the Detergent Micelle in Preserving the Structure of Membrane Proteins in the Gas Phase
Reading, E., Liko, I., Allison, T. M., Benesch, J. L. P., Laganowsky, A., & Robinson, C. V. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201411622 · Cited by 137
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Two decades of Martini: Better beads, broader scope
Marrink, S. J., Monticelli, L., Melo, M. N., Alessandri, R., Tieleman, D. P., & Souza, P. C. T. (2023) · WIREs Computational Molecular Science · doi:10.1002/wcms.1620 · Cited by 255
Novel roles of phosphoinositides in signaling, lipid transport, and disease
Hammond, G. R. V., & Burke, J. E. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.12.007 · Cited by 203
Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry
Chorev, D. S., Baker, L. A., Wu, D., Beilsten-Edmands, V., Rouse, S. L., Zeev-Ben-Mordehai, T., Jiko, C., Samsudin, F., Gerle, C., Khalid, S., et al. (2018) · Science · doi:10.1126/science.aau0976 · Cited by 191
Self-citationDirect protein-lipid interactions shape the conformational landscape of secondary transporters
Martens, C., Shekhar, M., Borysik, A. J., Lau, A. M., Reading, E., Tajkhorshid, E., Booth, P. J., & Politis, A. (2018) · Nature Communications · doi:10.1038/s41467-018-06704-1 · Cited by 134
Native Mass Spectrometry of Membrane Proteins
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Self-citationMass spectrometry: From plasma proteins to mitochondrial membranes
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Bunduc, C. M., Bitter, W., & Houben, E. N. G. (2020) · Annual Review of Microbiology · doi:10.1146/annurev-micro-012420-081657 · Cited by 50
Currie, M. J., Davies, J. S., Scalise, M., Gulati, A., Wright, J. D., Newton-Vesty, M. C., Abeysekera, G. S., Subramanian, R., Wahlgren, W. Y., Friemann, R., et al. (2024) · eLife · doi:10.7554/elife.92307.3 · Cited by 20
Self-citationmPPases create a conserved anionic membrane fingerprint as identified via multi-scale simulations
Holmes, A. O. M., Goldman, A., & Kalli, A. C. (2022) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1010578 · Cited by 3
Cryo‐EM structures of multiple‐peptide resistance factor ( MprF ) from Pseudomonas aeruginosa
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Metadata
- Authors
- Gupta, K., Donlan, J. A. C., Hopper, J. T. S., Uzdavinys, P., Landreh, M., Struwe, W. B., Drew, D., Baldwin, A. J., Stansfeld, P. J., & Robinson, C. V.
- Venue
- Nature
- Published
- 2017-01-11
- Volume
- 541
- Issue
- 7637
- Pages
- 421-424
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2578365017
- Cited by
- 401
- References
- 3
- FWCI
- 18.54
- Type
- journal article
- Language
- en
- Open access
- green
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