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- Title
Dimeric Tubulin Modifies Mechanical Properties of Lipid Bilayer, as Probed Using Gramicidin A Channel.
- Authors
Rostovtseva, Tatiana K.; Weinrich, Michael; Jacobs, Daniel; Rosencrans, William M.; Bezrukov, Sergey M.
- Abstract
Using the gramicidin A channel as a molecular probe, we show that tubulin binding to planar lipid membranes changes the channel kinetics—seen as an increase in the lifetime of the channel dimer—and thus points towards modification of the membrane's mechanical properties. The effect is more pronounced in the presence of non-lamellar lipids in the lipid mixture used for membrane formation. To interpret these findings, we propose that tubulin binding redistributes the lateral pressure of lipid packing along the membrane depth, making it closer to the profile expected for lamellar lipids. This redistribution happens because tubulin perturbs the lipid headgroup spacing to reach the membrane's hydrophobic core via its amphiphilic α-helical domain. Specifically, it increases the forces of repulsion between the lipid headgroups and reduces such forces in the hydrophobic region. We suggest that the effect is reciprocal, meaning that alterations in lipid bilayer mechanics caused by membrane remodeling during cell proliferation in disease and development may also modulate tubulin membrane binding, thus exerting regulatory functions. One of those functions includes the regulation of protein–protein interactions at the membrane surface, as exemplified by VDAC complexation with tubulin.
- Subjects
TUBULINS; BILAYER lipid membranes; LIPIDS; MEMBRANE lipids; MOLECULAR probes; PROTEIN-protein interactions; PROTEIN-lipid interactions
- Publication
International Journal of Molecular Sciences, 2024, Vol 25, Issue 4, p2204
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms25042204