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

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  • Yansong Miao

    (University of California
    School of Biological Sciences, Nanyang Technological University
    School of Chemical and Biomedical Engineering, Nanyang Technological University)

  • 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)

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.

Suggested Citation

  • Yansong Miao & Xuemei Han & Liangzhen Zheng & Ying Xie & Yuguang Mu & John R. Yates & David G. Drubin, 2016. "Fimbrin phosphorylation by metaphase Cdk1 regulates actin cable dynamics in budding yeast," Nature Communications, Nature, vol. 7(1), pages 1-12, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11265
    DOI: 10.1038/ncomms11265
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