The DOI matches its Crossref record; 71 of the 71 references it cites were found in a registry or an index.
Structural determinants and functional consequences of protein affinity for membrane rafts
Open accessAbstract
Eukaryotic plasma membranes are compartmentalized into functional lateral domains, including lipid-driven membrane rafts. Rafts are involved in most plasma membrane functions by selective recruitment and retention of specific proteins. However, the structural determinants of transmembrane protein partitioning to raft domains are not fully understood. Hypothesizing that protein transmembrane domains (TMDs) determine raft association, here we directly quantify raft affinity for dozens of TMDs. We identify three physical features that independently affect raft partitioning, namely TMD surface area, length, and palmitoylation. We rationalize these findings into a mechanistic, physical model that predicts raft affinity from the protein sequence. Application of these concepts to the human proteome reveals that plasma membrane proteins have higher raft affinity than those of intracellular membranes, consistent with raft-mediated plasma membrane sorting. Overall, our experimental observations and physical model establish general rules for raft partitioning of TMDs and support the central role of rafts in membrane traffic.
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VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,843
Polymorphic transitions in single crystals: A new molecular dynamics method
Parrinello, M., & Rahman, A. (1981) · Journal of Applied Physics · doi:10.1063/1.328693 · Cited by 19,790
Canonical sampling through velocity rescaling
Bussi, G., Donadio, D., & Parrinello, M. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2408420 · Cited by 18,089
GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
Hess, B., Kutzner, C., van der Spoel, D., & Lindahl, E. (2008) · Journal of Chemical Theory and Computation · doi:10.1021/ct700301q · Cited by 15,908
Krogh, A., Larsson, B., von Heijne, G., & Sonnhammer, E. L. L. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4315 · Cited by 12,654
Functional rafts in cell membranes
Simons, K., & Ikonen, E. (1997) · Nature · doi:10.1038/42408 · Cited by 9,757
The MARTINI Force Field: Coarse Grained Model for Biomolecular Simulations
Marrink, S. J., Risselada, H. J., Yefimov, S., Tieleman, D. P., & de Vries, A. H. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp071097f · Cited by 5,562
Evidence for the Formation of Symmetric and Asymmetric DLPC-DAPC Lipid Bilayer Domains
Ritter, M., Schmidt, S., Jakab, M., Paulmichl, M., & Henderson, R. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350122 · Cited by 3,923
Srimaroeng, C., Cecile, J. P., Walden, R., & Pritchard, J. B. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350077 · Cited by 2,989
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Plasma membranes are asymmetric in lipid unsaturation, packing and protein shape
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Self-citationRegulation of Transmembrane Signaling by Phase Separation
Case, L. B., Ditlev, J. A., & Rosen, M. K. (2019) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115534 · Cited by 303
Batrouni, A. G., Bag, N., Phan, H. T., Baird, B. A., & Baskin, J. M. (2022) · Journal of Cell Science · doi:10.1242/jcs.259365 · Cited by 24
Metadata
- Authors
- Lorent, J. H., Diaz-Rohrer, B., Lin, X., Spring, K., Gorfe, A. A., Levental, K. R., & Levental, I.
- Venue
- Nature Communications
- Published
- 2017-10-31
- Volume
- 8
- Issue
- 1
- Pages
- 1219-1219
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2766014895
- Cited by
- 283
- References
- 71
- FWCI
- 8.83
- Type
- journal article
- Language
- en
- Open access
- gold
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- Lorent, J. H., Diaz-Rohrer, B., Lin, X., Spring, K., Gorfe, A. A., Levental, K. R., & Levental, I. (2017). Structural determinants and functional consequences of protein affinity for membrane rafts. Nature Communications. https://doi.org/10.1038/s41467-017-01328-3
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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