Directional interactions and cooperativity between mechanosensitive membrane proteins
- Creators
- Haselwandter, Christoph A.
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Phillips, Rob
Abstract
While modern structural biology has provided us with a rich and diverse picture of membrane proteins, the biological function of membrane proteins is often influenced by the mechanical properties of the surrounding lipid bilayer. Here we explore the relation between the shape of membrane proteins and the cooperative function of membrane proteins induced by membrane-mediated elastic interactions. For the experimental model system of mechanosensitive ion channels we find that the sign and strength of elastic interactions depend on the protein shape, yielding distinct cooperative gating curves for distinct protein orientations. Our approach predicts how directional elastic interactions affect the molecular structure, organization, and biological function of proteins in crowded membranes.
Additional Information
© 2013 EPLA. Received 18 January 2013; accepted 25 February 2013; published online 26 March 2013. This work was supported at USC by the National Science Foundation through NSF award number DMR-1206332 and at Caltech by a Collaborative Innovation Award of the Howard Hughes Medical Institute, and the National Institutes of Health through NIH award number R01 GM084211 and the Director's Pioneer Award. We thank C. L. Henley, W. S. Klug, M. Lindén, D. C. Rees, and N. S. Wingreen for helpful comments.Attached Files
Accepted Version - nihms494041.pdf
Submitted - 1209.3083v2.pdf
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Additional details
- PMCID
- PMC4193682
- Eprint ID
- 38651
- Resolver ID
- CaltechAUTHORS:20130523-084817493
- NSF
- DMR-1206332
- Howard Hughes Medical Institute (HHMI) Collaborative Innovation Award
- NIH
- R01 GM084211
- NIH Director's Pioneer Award
- Created
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2013-06-03Created from EPrint's datestamp field
- Updated
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2022-07-12Created from EPrint's last_modified field