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Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
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Lipid organization by the Caveolin-1 complex.

Korbinian Liebl1, Gregory A Voth1

  • 1Department of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago, Chicago, Illinois.

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|September 22, 2024
PubMed
Summary
This summary is machine-generated.

Caveolins (CAV1) remodel cell membranes into caveolae, a process influenced by cholesterol. This study reveals how the CAV1-8S complex bends membranes and extracts cholesterol, with palmitoylation enhancing these effects.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Structural Biology

Background:

  • Caveolins are lipid-binding proteins crucial for membrane remodeling.
  • The CAV1-8S complex oligomerizes to form caveolae, structures dependent on cholesterol concentration.
  • The precise molecular mechanisms of membrane remodeling and cholesterol handling by caveolins remain unclear.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which the CAV1-8S complex induces membrane bending and accumulates cholesterol.
  • To investigate the role of CAV1 palmitoylations in these processes.
  • To evaluate the accuracy of coarse-grained force fields in simulating membrane bending by caveolins.

Main Methods:

  • Atomistic molecular dynamics simulations.
  • Advanced sampling techniques.
  • Backmapping to all-atom models from coarse-grained simulations.

Main Results:

  • The CAV1-8S complex bends lipid bilayers and accumulates cholesterol.
  • Palmitoylations on CAV1 enhance membrane bending and cholesterol accumulation.
  • The CAV1-8S complex can extract cholesterol from the lipid bilayer into its central beta barrel.
  • Atomistic simulations show localized membrane bending, contrasting with overestimation by the Martini v.2 coarse-grained force field.

Conclusions:

  • The CAV1-8S complex actively remodels membranes and filters cholesterol.
  • Palmitoylation is a key regulator of CAV1's membrane-associated functions.
  • Atomistic simulations provide a more accurate representation of membrane bending compared to certain coarse-grained models.