Dr Anders Aufderhorst-Roberts anders.aufderhorst-roberts@durham.ac.uk
Fixed Term Lectureship
Dr Anders Aufderhorst-Roberts anders.aufderhorst-roberts@durham.ac.uk
Fixed Term Lectureship
Dr Margarita Staykova margarita.staykova@durham.ac.uk
Associate Professor
The interaction between the actin cytoskeleton and the plasma membrane in eukaryotic cells is integral to a large number of functions such as shape change, mechanical reinforcement and contraction. These phenomena are driven by the architectural regulation of a thin actin network, directly beneath the membrane through interactions with a variety of binding proteins, membrane anchoring proteins and molecular motors. An increasingly common approach to understanding the mechanisms that drive these processes is to build model systems from reconstituted lipids, actin filaments and associated actin-binding proteins. Here we review recent progress in this field, with a particular emphasis on how the actin cytoskeleton provides mechanical reinforcement, drives shape change and induces contraction. Finally, we discuss potential future developments in the field, which would allow the extension of these techniques to more complex cellular processes.
Aufderhorst-Roberts, A., & Staykova, M. (2022). Scratching beyond the surface — minimal actin assemblies as tools to elucidate mechanical reinforcement and shape change. Emerging Topics in Life Sciences, 6(6), 583-592. https://doi.org/10.1042/etls20220052
Journal Article Type | Article |
---|---|
Acceptance Date | Dec 9, 2022 |
Online Publication Date | Dec 21, 2022 |
Publication Date | 2022-12 |
Deposit Date | Jan 9, 2023 |
Publicly Available Date | Jan 9, 2023 |
Journal | Emerging Topics in Life Sciences |
Print ISSN | 2397-8554 |
Electronic ISSN | 2397-8562 |
Publisher | Portland Press |
Peer Reviewed | Peer Reviewed |
Volume | 6 |
Issue | 6 |
Pages | 583-592 |
DOI | https://doi.org/10.1042/etls20220052 |
Published Journal Article
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http://creativecommons.org/licenses/by/4.0/
Copyright Statement
This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and the Royal Society of Biology and distributed under the Creative Commons Attribution License 4.0 (CC BY). Open access for this article was enabled by the participation of Durham University in an all-inclusive Read & Publish agreement with Portland Press and the Biochemical Society under a transformative agreement with JISC.
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