Author
Listed:
- Miao Yu
(Mechanobiology Institute, National University of Singapore
National University of Singapore)
- Xin Yuan
(Mechanobiology Institute, National University of Singapore)
- Chen Lu
(Mechanobiology Institute, National University of Singapore)
- Shimin Le
(Mechanobiology Institute, National University of Singapore
National University of Singapore)
- Ryo Kawamura
(Mechanobiology Institute, National University of Singapore
National University of Singapore)
- Artem K. Efremov
(Mechanobiology Institute, National University of Singapore)
- Zhihai Zhao
(Mechanobiology Institute, National University of Singapore
National University of Singapore)
- Michael M. Kozlov
(Tel Aviv University)
- Michael Sheetz
(Mechanobiology Institute, National University of Singapore
Columbia University)
- Alexander Bershadsky
(Mechanobiology Institute, National University of Singapore
Weizmann Institute of Science)
- Jie Yan
(Mechanobiology Institute, National University of Singapore
National University of Singapore
National University of Singapore)
Abstract
Formins, an important family of force-bearing actin-polymerizing factors, function as homodimers that bind with the barbed end of actin filaments through a ring-like structure assembled from dimerized FH2 domains. It has been hypothesized that force applied to formin may facilitate transition of the FH2 ring from an inhibitory closed conformation to a permissive open conformation, speeding up actin polymerization. We confirm this hypothesis for mDia1 dependent actin polymerization by stretching a single-actin filament in the absence of profilin using magnetic tweezers, and observe that increasing force from 0.5 to 10 pN can drastically speed up the actin polymerization rate. Further, we find that this force-promoted actin polymerization requires torsionally unconstrained actin filament, suggesting that mDia1 also senses torque. As actin filaments are subject to complex mechanical constraints in living cells, these results provide important insights into how formin senses these mechanical constraints and regulates actin organization accordingly.
Suggested Citation
Miao Yu & Xin Yuan & Chen Lu & Shimin Le & Ryo Kawamura & Artem K. Efremov & Zhihai Zhao & Michael M. Kozlov & Michael Sheetz & Alexander Bershadsky & Jie Yan, 2017.
"mDia1 senses both force and torque during F-actin filament polymerization,"
Nature Communications, Nature, vol. 8(1), pages 1-9, December.
Handle:
RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01745-4
DOI: 10.1038/s41467-017-01745-4
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Cited by:
- Yee Han Tee & Wei Jia Goh & Xianbin Yong & Hui Ting Ong & Jinrong Hu & Ignacius Yan Yun Tay & Shidong Shi & Salma Jalal & Samuel F. H. Barnett & Pakorn Kanchanawong & Wenmao Huang & Jie Yan & Yong Ann, 2023.
"Actin polymerisation and crosslinking drive left-right asymmetry in single cell and cell collectives,"
Nature Communications, Nature, vol. 14(1), pages 1-17, December.
- Sayaka Sekine & Mitsusuke Tarama & Housei Wada & Mustafa M. Sami & Tatsuo Shibata & Shigeo Hayashi, 2024.
"Emergence of periodic circumferential actin cables from the anisotropic fusion of actin nanoclusters during tubulogenesis,"
Nature Communications, Nature, vol. 15(1), pages 1-13, December.
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