Journal
SOFT MATTER
Volume 18, Issue 17, Pages 3384-3394Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d2sm00274d
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Funding
- JSPS KAKENHI [JP21K03481]
- European Research Council [CoG-681434]
- European Commission [H2020-FETPROACT-01-2016-731957]
- Spanish Ministry for Science and Innovation/FEDER [PID2019-110949GBI00, BES-2016-078220]
- Generalitat de Catalunya (ICREA Academia award)
- National Science Foundation through the KITP program: The Physics of Elastic Films: from Biological Membranes to Extreme Mechanics (FILMS21) [NSF PHY-1748958]
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This study investigates how anisotropic proteins bind and orient themselves on membrane tubes, showing transitions in protein density and tube radius, as well as changes in protein orientation under external forces. The findings provide insights into the behavior of these proteins on biomembranes.
Bin/Amphiphysin/Rvs superfamily proteins and other curvature-inducing proteins have anisotropic shapes and anisotropically bend biomembranes. Here, we report how the anisotropic proteins bind the membrane tube and are orientationally ordered using mean-field theory including an orientation-dependent excluded volume. The proteins exhibit a second-order or first-order nematic transition with increasing protein density depending on the radius of the membrane tube. The tube curvatures for the maximum protein binding and orientational order are different and varied by the protein density and rigidity. As the external force along the tube axis increases, a first-order transition from a large tube radius with low protein density to a small radius with high density occurs once, and subsequently, the protein orientation tilts to the tube-axis direction. When an isotropic bending energy is used for the proteins with an elliptic shape, the force-dependence curves become symmetric and the first-order transition occurs twice. This theory quantitatively reproduces the results of meshless membrane simulation for short proteins, whereas deviations are seen for long proteins owing to the formation of protein clusters.
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