Profilin and formin constitute a pacemaker system for robust actin filament growth
The actin cytoskeleton drives many essential biological processes, from cell morphogenesis to motility. Assembly of functional actin networks requires control over the speed at which actin filaments grow. How this can be achieved at the high and variable levels of soluble actin subunits found in cel...
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doaj-f637458022114ee2ab8bf5b3ebccbb8f2021-05-05T18:02:17ZengeLife Sciences Publications LtdeLife2050-084X2019-10-01810.7554/eLife.50963Profilin and formin constitute a pacemaker system for robust actin filament growthJohanna Funk0https://orcid.org/0000-0003-1214-8531Felipe Merino1https://orcid.org/0000-0003-4166-8747Larisa Venkova2https://orcid.org/0000-0001-5721-7962Lina Heydenreich3Jan Kierfeld4https://orcid.org/0000-0003-4291-0638Pablo Vargas5Stefan Raunser6https://orcid.org/0000-0001-9373-3016Matthieu Piel7Peter Bieling8https://orcid.org/0000-0002-7458-4358Department of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, GermanyDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, GermanyInstitut Curie UMR144 CNRS, Paris, FrancePhysics Department, TU Dortmund University, Dortmund, GermanyPhysics Department, TU Dortmund University, Dortmund, GermanyInstitut Curie UMR144 CNRS, Paris, FranceDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, GermanyInstitut Curie UMR144 CNRS, Paris, FranceDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, GermanyThe actin cytoskeleton drives many essential biological processes, from cell morphogenesis to motility. Assembly of functional actin networks requires control over the speed at which actin filaments grow. How this can be achieved at the high and variable levels of soluble actin subunits found in cells is unclear. Here we reconstitute assembly of mammalian, non-muscle actin filaments from physiological concentrations of profilin-actin. We discover that under these conditions, filament growth is limited by profilin dissociating from the filament end and the speed of elongation becomes insensitive to the concentration of soluble subunits. Profilin release can be directly promoted by formin actin polymerases even at saturating profilin-actin concentrations. We demonstrate that mammalian cells indeed operate at the limit to actin filament growth imposed by profilin and formins. Our results reveal how synergy between profilin and formins generates robust filament growth rates that are resilient to changes in the soluble subunit concentration.https://elifesciences.org/articles/50963cytokeletonactinpolymerizationpolymeraseprofilinformin |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Johanna Funk Felipe Merino Larisa Venkova Lina Heydenreich Jan Kierfeld Pablo Vargas Stefan Raunser Matthieu Piel Peter Bieling |
spellingShingle |
Johanna Funk Felipe Merino Larisa Venkova Lina Heydenreich Jan Kierfeld Pablo Vargas Stefan Raunser Matthieu Piel Peter Bieling Profilin and formin constitute a pacemaker system for robust actin filament growth eLife cytokeleton actin polymerization polymerase profilin formin |
author_facet |
Johanna Funk Felipe Merino Larisa Venkova Lina Heydenreich Jan Kierfeld Pablo Vargas Stefan Raunser Matthieu Piel Peter Bieling |
author_sort |
Johanna Funk |
title |
Profilin and formin constitute a pacemaker system for robust actin filament growth |
title_short |
Profilin and formin constitute a pacemaker system for robust actin filament growth |
title_full |
Profilin and formin constitute a pacemaker system for robust actin filament growth |
title_fullStr |
Profilin and formin constitute a pacemaker system for robust actin filament growth |
title_full_unstemmed |
Profilin and formin constitute a pacemaker system for robust actin filament growth |
title_sort |
profilin and formin constitute a pacemaker system for robust actin filament growth |
publisher |
eLife Sciences Publications Ltd |
series |
eLife |
issn |
2050-084X |
publishDate |
2019-10-01 |
description |
The actin cytoskeleton drives many essential biological processes, from cell morphogenesis to motility. Assembly of functional actin networks requires control over the speed at which actin filaments grow. How this can be achieved at the high and variable levels of soluble actin subunits found in cells is unclear. Here we reconstitute assembly of mammalian, non-muscle actin filaments from physiological concentrations of profilin-actin. We discover that under these conditions, filament growth is limited by profilin dissociating from the filament end and the speed of elongation becomes insensitive to the concentration of soluble subunits. Profilin release can be directly promoted by formin actin polymerases even at saturating profilin-actin concentrations. We demonstrate that mammalian cells indeed operate at the limit to actin filament growth imposed by profilin and formins. Our results reveal how synergy between profilin and formins generates robust filament growth rates that are resilient to changes in the soluble subunit concentration. |
topic |
cytokeleton actin polymerization polymerase profilin formin |
url |
https://elifesciences.org/articles/50963 |
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