Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Calponin-homology domain mediated bending of membrane-associated actin filaments

Tools
- Tools
+ Tools

Palani, Saravanan, Ghosh, Sayantika, Ivorra-Molla, Esther, Clarke, Scott T., Suchenko, Andrejus, Balasubramanian, Mohan K. and Köster, Darius Vasco (2021) Calponin-homology domain mediated bending of membrane-associated actin filaments. eLife, 10 . e61078. doi:10.7554/eLife.61078

[img]
Preview
PDF
WRAP-Calponin-homology-domain-mediated-bending-membrane-associated-actin-filaments-Köster-2021.pdf - Published Version - Requires a PDF viewer.
Available under License Creative Commons Attribution 4.0.

Download (2317Kb) | Preview
Official URL: http://dx.doi.org/10.7554/eLife.61078

Request Changes to record.

Abstract

Actin filaments are central to numerous biological processes in all domains of life. Driven by the interplay with molecular motors, actin binding and actin modulating proteins, the actin cytoskeleton exhibits a variety of geometries. This includes structures with a curved geometry such as axon-stabilizing actin rings, actin cages around mitochondria and the cytokinetic actomyosin ring, which are generally assumed to be formed by short linear filaments held together by actin cross-linkers. However, whether individual actin filaments in these structures could be curved and how they may assume a curved geometry remains unknown. Here, we show that ‘curly’, a region from the IQGAP family of proteins from three different organisms, comprising the actin-binding calponin-homology domain and a C-terminal unstructured domain, stabilizes individual actin filaments in a curved geometry when anchored to lipid membranes. Although F-actin is semi-flexible with a persistence length of ~10 μm, binding of mobile curly within lipid membranes generates actin filament arcs and full rings of high curvature with radii below 1 μm. Higher rates of fully formed actin rings are observed in the presence of the actin-binding coiled-coil protein tropomyosin and when actin is directly polymerized on lipid membranes decorated with curly. Strikingly, curly induced actin filament rings contract upon the addition of muscle myosin II filaments and expression of curly in mammalian cells leads to highly curved actin structures in the cytoskeleton. Taken together, our work identifies a new mechanism to generate highly curved actin filaments, which opens a range of possibilities to control actin filament geometries, that can be used, for example, in designing synthetic cytoskeletal structures.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Divisions: Faculty of Medicine > Warwick Medical School > Biomedical Sciences > Cell & Developmental Biology
Faculty of Medicine > Warwick Medical School > Biomedical Sciences
Faculty of Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Microfilament proteins, Actin, Cytology
Journal or Publication Title: eLife
Publisher: eLife Sciences Publications Ltd.
ISSN: 2050-084X
Official Date: 16 July 2021
Dates:
DateEvent
16 July 2021Published
15 July 2021Accepted
Volume: 10
Article Number: e61078
DOI: 10.7554/eLife.61078
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
WT 101885MAWellcome Trusthttp://dx.doi.org/10.13039/100010269
ERC-2014-ADG N˚ 671083Horizon 2020 Framework Programmehttp://dx.doi.org/10.13039/100010661
ISSF-Warwick QBP RMRCB0058Wellcome Trusthttp://dx.doi.org/10.13039/100010269
DBT-IISc partnership grant Department of Biotechnology , Ministry of Science and Technologyhttp://dx.doi.org/10.13039/501100001407
Research development fund - RD19012University of Warwickhttp://dx.doi.org/10.13039/501100000741
International Chancellor’s FellowshipUniversity of Warwickhttp://dx.doi.org/10.13039/501100000741
ARAP fellowshipUniversity of Warwickhttp://dx.doi.org/10.13039/501100000741

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics

twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us