Membrane Charge Directs the Outcome of F-BAR Domain Lipid Binding and Autoregulation
| Autor: | Michael F. Hagan, Agata N. Becalska, Tania L. Eskin, Dganit Danino, ShiYu Wang, Oleg Shupliakov, Kangkang Song, Kalanit Vishnia, Olga Sokolova, Charlotte F. Kelley, Daniela Nicastro, Emily M. Messelaar, Avital A. Rodal |
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| Rok vydání: | 2015 |
| Předmět: |
Cellular membrane
Lipid composition F-BAR domain Static Electricity Biology Bioinformatics Article General Biochemistry Genetics and Molecular Biology SH3 domain src Homology Domains PI(4 5)P2 Lipid binding Animals Drosophila Proteins BAR domain Autoregulation lcsh:QH301-705.5 Nwk membrane Phospholipids Microscopy Confocal Cell Membrane Protein Structure Tertiary Membrane lcsh:Biology (General) Membrane curvature Larva Liposomes Biophysics Drosophila Carrier Proteins Dimerization Protein Binding |
| Zdroj: | Cell Reports, Vol 13, Iss 11, Pp 2597-2609 (2015) |
| ISSN: | 2211-1247 |
| DOI: | 10.1016/j.celrep.2015.11.044 |
| Popis: | SummaryF-BAR domain proteins regulate and sense membrane curvature by interacting with negatively charged phospholipids and assembling into higher-order scaffolds. However, regulatory mechanisms controlling these interactions are poorly understood. Here, we show that Drosophila Nervous Wreck (Nwk) is autoregulated by a C-terminal SH3 domain module that interacts directly with its F-BAR domain. Surprisingly, this autoregulation does not mediate a simple “on-off” switch for membrane remodeling. Instead, the isolated Nwk F-BAR domain efficiently assembles into higher-order structures and deforms membranes only within a limited range of negative membrane charge, and autoregulation elevates this range. Thus, autoregulation could either reduce membrane binding or promote higher-order assembly, depending on local cellular membrane composition. Our findings uncover an unexpected mechanism by which lipid composition directs membrane remodeling. |
| Databáze: | OpenAIRE |
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