Unknown

Dataset Information

0

Membrane curvature and its generation by BAR proteins.


ABSTRACT: Membranes are flexible barriers that surround the cell and its compartments. To execute vital functions such as locomotion or receptor turnover, cells need to control the shapes of their membranes. In part, this control is achieved through membrane-bending proteins, such as the Bin/amphiphysin/Rvs (BAR) domain proteins. Many open questions remain about the mechanisms by which membrane-bending proteins function. Addressing this shortfall, recent structures of BAR protein:membrane complexes support existing mechanistic models, but also produced novel insights into how BAR domain proteins sense, stabilize, and generate curvature. Here we review these recent findings, focusing on how BAR proteins interact with the membrane, and how the resulting scaffold structures might aid the recruitment of other proteins to the sites where membranes are bent.

SUBMITTER: Mim C 

PROVIDER: S-EPMC3508348 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Membrane curvature and its generation by BAR proteins.

Mim Carsten C   Unger Vinzenz M VM  

Trends in biochemical sciences 20121008 12


Membranes are flexible barriers that surround the cell and its compartments. To execute vital functions such as locomotion or receptor turnover, cells need to control the shapes of their membranes. In part, this control is achieved through membrane-bending proteins, such as the Bin/amphiphysin/Rvs (BAR) domain proteins. Many open questions remain about the mechanisms by which membrane-bending proteins function. Addressing this shortfall, recent structures of BAR protein:membrane complexes suppor  ...[more]

Similar Datasets

| S-EPMC7261005 | biostudies-literature
| S-EPMC8642264 | biostudies-literature
| S-EPMC7835363 | biostudies-literature
| S-EPMC1500843 | biostudies-literature
| S-EPMC10702824 | biostudies-literature
| S-EPMC2888429 | biostudies-literature
| S-EPMC3519285 | biostudies-literature
| S-SCDT-10_15252-EMBR_202357232 | biostudies-other
| S-EPMC2776096 | biostudies-literature
| S-EPMC4021884 | biostudies-literature