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Chlamydomonas reinhardtii formin and profilin are optimized for acute rapid actin filament assembly

View ORCID ProfileJenna R. Christensen, Michael J. Glista, David M. Mueller, Yujie Li, Jennifer A. Sees, Colleen T. Skau, Laurens J. Mets, View ORCID ProfilePrachee Avasthi, David R. Kovar
doi: https://doi.org/10.1101/096008
Jenna R. Christensen
aDepartment of Molecular Genetics and Cell Biology The University of Chicago, Chicago, IL 60637, USA
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Michael J. Glista
aDepartment of Molecular Genetics and Cell Biology The University of Chicago, Chicago, IL 60637, USA
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David M. Mueller
bDepartment of Anatomy and Cell Biology University of Kansas Medical Center, Kansas City, KS 66103
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Yujie Li
aDepartment of Molecular Genetics and Cell Biology The University of Chicago, Chicago, IL 60637, USA
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Jennifer A. Sees
aDepartment of Molecular Genetics and Cell Biology The University of Chicago, Chicago, IL 60637, USA
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Colleen T. Skau
aDepartment of Molecular Genetics and Cell Biology The University of Chicago, Chicago, IL 60637, USA
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Laurens J. Mets
aDepartment of Molecular Genetics and Cell Biology The University of Chicago, Chicago, IL 60637, USA
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Prachee Avasthi
bDepartment of Anatomy and Cell Biology University of Kansas Medical Center, Kansas City, KS 66103
cDepartment of Ophthalmology University of Kansas Medical Center, Kansas City, KS 66103
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  • For correspondence: pavasthi@kumc.edu drkovar@uchicago.edu
David R. Kovar
aDepartment of Molecular Genetics and Cell Biology The University of Chicago, Chicago, IL 60637, USA
dDepartment of Biochemistry and Molecular Biology The University of Chicago, Chicago, IL 60637, USA
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  • For correspondence: pavasthi@kumc.edu drkovar@uchicago.edu
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ABSTRACT

Chlamydomonas reinhardtii is a unicellular green alga that appears less dependent upon a conventional actin cytoskeleton than other eukaryotes, in part due to overlapping functions of a second non-conventional actin. One network that contains exclusively conventional F-actin is the fertilization tubule, a mating structure at the apical cell surface in gametes. Therefore, Chlamydomonas is an excellent system to investigate how actin polymerization is regulated in space and time. Chlamydomonas expresses a profilin (CrPRF), and a formin (CrFor1) that we have characterized for the first time. We found that unlike typical profilins, CrPRF prevents unwanted actin assembly by strongly inhibiting both F-actin nucleation and barbed end elongation at equimolar concentrations to actin. However, CrFor1 is able to stimulate rapid actin filament assembly of CrPRF-bound actin. CrPRF further favors CrFor1-mediated actin assembly by potently inhibiting Arp2/3 complex-mediated actin assembly. The small molecule formin inhibitor SMIFH2 prevents fertilization tubule formation in gametes, suggesting that mating is a primary function of CrFor1. Together, these findings indicate that CrFor1 and CrPRF cooperate to selectively and rapidly assemble F-actin at the right time and place.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC 4.0 International license.
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Posted February 09, 2017.
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Chlamydomonas reinhardtii formin and profilin are optimized for acute rapid actin filament assembly
Jenna R. Christensen, Michael J. Glista, David M. Mueller, Yujie Li, Jennifer A. Sees, Colleen T. Skau, Laurens J. Mets, Prachee Avasthi, David R. Kovar
bioRxiv 096008; doi: https://doi.org/10.1101/096008
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Chlamydomonas reinhardtii formin and profilin are optimized for acute rapid actin filament assembly
Jenna R. Christensen, Michael J. Glista, David M. Mueller, Yujie Li, Jennifer A. Sees, Colleen T. Skau, Laurens J. Mets, Prachee Avasthi, David R. Kovar
bioRxiv 096008; doi: https://doi.org/10.1101/096008

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