Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly.
作者： Dennis Zimmermann , Kaitlin E. Homa , Glen M. Hocky , Luther W. Pollard , Enrique M. De La Cruz
DOI: 10.1038/S41467-017-00445-3
关键词:
摘要: Cytokinesis physically separates dividing cells by forming a contractile actomyosin ring. The fission yeast ring has been proposed to assemble Search-Capture-Pull-Release from cytokinesis precursor nodes that include the molecular motor type-II myosin Myo2 and actin assembly factor formin Cdc12. By successfully reconstituting Search-Capture-Pull in vitro, we discovered Cdc12 is mechanosensor, whereby pulling on formin-bound filaments inhibits Cdc12-mediated assembly. We mapped mechanoregulation its homology 1 domain, which facilitates delivery of new subunits elongating filament. Quantitative modeling suggests force propagates through filament, behaves as an entropic spring, thereby may stretch disordered domain impede formin-mediated filament elongation. Finally, live cell imaging mechano-insensitive mutant established required for efficient vivo. cytokinetic assembles Myo2. authors reconstitute vitro find Cdc12-associated mechano-inhibits assembly, enables proper
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