English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Phospholipid Scramblases Remodel the Shape of Asymmetric Membranes

MPS-Authors
/persons/resource/persons238046

Siggel,  Marc
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

Bhaskara,  Ramachandra M.
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons15259

Hummer,  Gerhard       
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Insitute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Siggel, M., Bhaskara, R. M., & Hummer, G. (2019). Phospholipid Scramblases Remodel the Shape of Asymmetric Membranes. The Journal of Physical Chemistry Letters, 10(20), 6351-6354. doi:10.1021/acs.jpclett.9b02531.


Cite as: https://hdl.handle.net/21.11116/0000-0004-F4CE-1
Abstract
The cell membrane and many organellar membranes are asymmetric and highly curved. In experiments, it is challenging to reconstitute and characterize membranes that differ in the lipid composition of their leaflets. Here we use molecular dynamics simulations to study the large-scale membrane shape changes associated with lipid shuttling between asymmetric leaflets. We exploit leaflet asymmetry to create a stable, near-spherical vesicle bud connected to a flat bilayer under periodic boundary conditions. Then we demonstrate how the lipid scramblase nhTMEM16 relaxes the lipid-number asymmetry. By mediating the flipping of lipids, this transmembrane protein dissipates the mechanochemical gradient between the leaflets and drives a large-scale membrane reorganization, converting the vesicle bud into a flat membrane. Our procedure to exploit bilayer asymmetry for simulations of highly curved membranes can be used to study the function of other lipid transporters and membrane-shaping proteins.