Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy
| Author(s) | Yehl, Jenna | |
| Author(s) | Kudryashova, Elena | |
| Author(s) | Reisler, Emil | |
| Author(s) | Kudryashov, Dmitri | |
| Author(s) | Polenova, Tatyana | |
| Ordered Author | Jenna Yehl, Elena Kudryashova, Emil Reisler, Dmitri Kudryashov & Tatyana Polenova | |
| UD Author | Polenova, Tatyana | en_US |
| Date Accessioned | 2018-08-08T14:25:25Z | |
| Date Available | 2018-08-08T14:25:25Z | |
| Copyright Date | Copyright © The Author(s) 2017. | en_US |
| Publication Date | 2017-03-17 | |
| Description | Publisher's PDF | en_US |
| Abstract | Cellular actin dynamics is an essential element of numerous cellular processes, such as cell motility, cell division and endocytosis. Actin’s involvement in these processes is mediated by many actinbinding proteins, among which the cofilin family plays unique and essential role in accelerating actin treadmilling in filamentous actin (F-actin) in a nucleotide-state dependent manner. Cofilin preferentially interacts with older filaments by recognizing time-dependent changes in F-actin structure associated with the hydrolysis of ATP and release of inorganic phosphate (Pi) from the nucleotide cleft of actin. The structure of cofilin on F-actin and the details of the intermolecular interface remain poorly understood at atomic resolution. Here we report atomic-level characterization by magic angle spinning (MAS) NMR of the muscle isoform of human cofilin 2 (CFL2) bound to F-actin. We demonstrate that resonance assignments for the majority of atoms are readily accomplished and we derive the intermolecular interface between CFL2 and F-actin. The MAS NMR approach reported here establishes the foundation for atomic-resolution characterization of a broad range of actin-associated proteins bound to F-actin. | en_US |
| Department | University of Delaware. Department of Chemistry and Biochemistry. | en_US |
| Citation | Yehl, J. et al. Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy. Sci. Rep. 7, 44506; doi: 10.1038/ srep44506 (2017). | en_US |
| DOI | 10.1038/srep44506 | en_US |
| ISSN | 2045-2322 | en_US |
| URL | http://udspace.udel.edu/handle/19716/23664 | |
| Language | en_US | en_US |
| Publisher | Nature Publishing Group | en_US |
| dc.rights | Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. | en_US |
| dc.rights | This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license. | en_US |
| dc.source | Scientific Reports | en_US |
| dc.source.uri | https://www.nature.com/srep/ | en_US |
| Title | Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy | en_US |
| Type | Article | en_US |
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