Long-Range Organization of Membrane-Curving Proteins
| Autor: | Gregory A. Voth, Mijo Simunovic, Ka Yee C. Lee, J. Michael Henderson, Anđela Šarić |
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| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Range (particle radiation) Chemistry Atomic force microscopy General Chemical Engineering Biological membrane 02 engineering and technology General Chemistry 021001 nanoscience & nanotechnology Cell biology Protein filament lcsh:Chemistry 03 medical and health sciences 030104 developmental biology Membrane lcsh:QD1-999 Amphiphysin Membrane remodeling 0210 nano-technology Lipid bilayer Research Article |
| Zdroj: | ACS Central Science, Vol 3, Iss 12, Pp 1246-1253 (2017) ACS Central Science |
| ISSN: | 2374-7951 2374-7943 |
| Popis: | Biological membranes have a central role in mediating the organization of membrane-curving proteins, a dynamic process that has proven to be challenging to probe experimentally. Using atomic force microscopy, we capture the hierarchically organized assemblies of Bin/amphiphysin/Rvs (BAR) proteins on supported lipid membranes. Their structure reveals distinct long linear aggregates of proteins, regularly spaced by up to 300 nm. Employing accurate free-energy calculations from large-scale coarse-grained computer simulations, we found that the membrane mediates the interaction among protein filaments as a combination of short- and long-ranged interactions. The long-ranged component acts at strikingly long distances, giving rise to a variety of micron-sized ordered patterns. This mechanism may contribute to the long-ranged spatiotemporal control of membrane remodeling by proteins in the cell. High-resolution imaging and free-energy simulations reveal unexpected long-ranged interactions between filaments of membrane-curving proteins. |
| Databáze: | OpenAIRE |
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