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A biochemical network controlling basal myosin oscillation
Xiang Qin, Edouard Hannezo, Thomas Mangeat, Chang Liu, Pralay Majumder, Jiaying Liu, Valerie Choesmel-Cadamuro, Jocelyn Mcdonald, Yiyao Liu, Bin Yi, Xiaobo Wang

A biochemical network controlling basal myosin oscillation

Science & Mathematics Published 2018 Verification Pending

Overview & Synopsis

The actomyosin cytoskeleton, a key stress-producing unit in epithelial cells, oscillates spontaneously in a wide variety of systems. Although much of the signal cascade regulating myosin activity has been characterized, the origin of such oscillatory behavior is still unclear. Here, we show that basal myosin II oscillation in Drosophila ovarian epithelium is not controlled by actomyosin cortical tension, but instead relies on a biochemical oscillator involving ROCK and myosin phosphatase. Key to this oscillation is a diffusive ROCK flow, linking junctional Rho1 to medial actomyosin cortex, and dynamically maintained by a self-activation loop reliant on ROCK kinase activity. In response to the resulting myosin II recruitment, myosin phosphatase is locally enriched and shuts off ROCK and myosin II signals. Coupling Drosophila genetics, live imaging, modeling, and optogenetics, we uncover an intrinsic biochemical oscillator at the core of myosin II regulatory network, shedding light on the spatio-temporal dynamics of force generation.

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Document Information

Document Title A biochemical network controlling basal myosin oscillation
Author / Organization Xiang Qin, Edouard Hannezo, Thomas Mangeat, Chang Liu, Pralay Majumder, Jiaying Liu, Valerie Choesmel-Cadamuro, Jocelyn Mcdonald, Yiyao Liu, Bin Yi, Xiaobo Wang
Subject & Discipline Multidisciplinary Academic Open Research
Categories Science & Mathematics
Publication Year 2018
License / Rights Open Access / Creative Commons
Resource Verification Listed PDF (Verification Pending)
Original Host Website HAL Open Science (hal.science)
File Format application/pdf (Portable Document Format)
Language EN
Catalog ID DOC-137180
Original Source Link Visit Source Page on hal.science »