Fimbrin phosphorylation by metaphase Cdk1 regulates actin cable dynamics in budding yeast

Yansong Miao (), Xuemei Han, Liangzhen Zheng, Ying Xie, Yuguang Mu, John R. Yates and David G. Drubin ()
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Yansong Miao: University of California
Xuemei Han: The Scripps Research Institute
Liangzhen Zheng: School of Biological Sciences, Nanyang Technological University
Ying Xie: School of Chemical and Biomedical Engineering, Nanyang Technological University
Yuguang Mu: School of Biological Sciences, Nanyang Technological University
John R. Yates: The Scripps Research Institute
David G. Drubin: University of California

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract Actin cables, composed of actin filament bundles nucleated by formins, mediate intracellular transport for cell polarity establishment and maintenance. We previously observed that metaphase cells preferentially promote actin cable assembly through cyclin-dependent kinase 1 (Cdk1) activity. However, the relevant metaphase Cdk1 targets were not known. Here we show that the highly conserved actin filament crosslinking protein fimbrin is a critical Cdk1 target for actin cable assembly regulation in budding yeast. Fimbrin is specifically phosphorylated on threonine 103 by the metaphase cyclin–Cdk1 complex, in vivo and in vitro. On the basis of conformational simulations, we suggest that this phosphorylation stabilizes fimbrin’s N-terminal domain, and modulates actin filament binding to regulate actin cable assembly and stability in cells. Overall, this work identifies fimbrin as a key target for cell cycle regulation of actin cable assembly in budding yeast, and suggests an underlying mechanism.

Date: 2016
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DOI: 10.1038/ncomms11265

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