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

Palani, Saravanan, Ghosh, Sayantika, Ivorra-Molla, Esther, Clarke, Scott, Suchenko, Andrejus, Balasubramanian, Mohan K, Köster, Darius Vasco·2021·eLife
DOI 10.7554/elife.61078

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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.

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Metadata

Authors
Palani, S., Ghosh, S., Ivorra-Molla, E., Clarke, S., Suchenko, A., Balasubramanian, M. K., & Köster, D. V.
Affiliations
Centre for Mechanochemical Cell Biology and Warwick Medical School, Division of Biomedical Sciences, Coventry, United Kingdom
ORCID
Venue
eLife
Publisher
eLife Sciences Publications, Ltd
Published
2021-07-16
Volume
10
ISSN
2050-084X
DOI
10.7554/elife.61078
Cited by
31
References
0
Language
en
Licence
Funders
  • Wellcome Trust (WT 101885MA, ISSF-Warwick QBP RMRCB0058)
  • H2020 European Research Council (ERC-2014-ADG N° 671083)
  • Department of Biotechnology, Ministry of Science and Technology, India (DBT-IISc partnership grant)
  • University of Warwick (Research development fund - RD19012, International Chancellor's Fellowship, ARAP fellowship)

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Palani, S., Ghosh, S., Ivorra-Molla, E., Clarke, S., Suchenko, A., Balasubramanian, M. K., & Köster, D. V. (2021). Calponin-homology domain mediated bending of membrane-associated actin filaments. eLife. https://doi.org/10.7554/elife.61078

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