Synergy between intrinsically disordered domains and structured proteins amplifies membrane curvature sensing
| Autor: | Wilton T. Snead, Andre C.M. DeGroot, D. Thirumalai, Wade F. Zeno, Eileen M. Lafer, Jeanne C. Stachowiak, Liping Wang, Upayan Baul |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Membrane Fluidity Science Entropy Lipid Bilayers Protein domain General Physics and Astronomy Curvature Condensed Matter::Disordered Systems and Neural Networks Protein Structure Secondary Article General Biochemistry Genetics and Molecular Biology Quantitative Biology::Cell Behavior Cell Line Quantitative Biology::Subcellular Processes 03 medical and health sciences 0302 clinical medicine Protein structure Protein Domains Membrane fluidity Humans lcsh:Science Unilamellar Liposomes Physics Quantitative Biology::Biomolecules Microscopy Confocal Multidisciplinary Cell Membrane Membrane Proteins General Chemistry Conformational entropy Intrinsically Disordered Proteins 030104 developmental biology Membrane Membrane curvature Biophysics lcsh:Q Mathematics::Differential Geometry Algorithms 030217 neurology & neurosurgery Entropy (order and disorder) |
| Zdroj: | Nature Communications Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018) |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-018-06532-3 |
| Popis: | The ability of proteins to sense membrane curvature is essential to cellular function. All known sensing mechanisms rely on protein domains with specific structural features such as wedge-like amphipathic helices and crescent-shaped BAR domains. Yet many proteins that contain these domains also contain large intrinsically disordered regions. Here we report that disordered domains are themselves potent sensors of membrane curvature. Comparison of Monte Carlo simulations with in vitro and live-cell measurements demonstrates that the polymer-like behavior of disordered domains found in endocytic proteins drives them to partition preferentially to convex membrane surfaces, which place fewer geometric constraints on their conformational entropy. Further, proteins containing both structured curvature sensors and disordered regions are more than twice as curvature sensitive as their respective structured domains alone. These findings demonstrate an entropic mechanism of curvature sensing that is independent of protein structure and illustrate how structured and disordered domains can synergistically enhance curvature sensitivity. Many proteins which sense membrane curvature contain intrinsically disordered domains. Here the authors use Monte Carlo simulations combined with experimental approaches and report that disordered domains are potent sensors of membrane curvature. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|