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

Academic Article
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Overview

authors

  • Miao, Y.
  • Han, X.
  • Zheng, L.
  • Xie, Y.
  • Mu, Y.
  • Yates III, John
  • Drubin, D. G.

publication date

  • April 2016

journal

  • Nature Communications  Journal

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.

subject areas

  • Actins
  • CDC2 Protein Kinase
  • Computer Simulation
  • Cyclins
  • Membrane Glycoproteins
  • Metaphase
  • Microfilament Proteins
  • Mutation
  • Phosphorylation
  • Phosphothreonine
  • Protein Binding
  • Protein Structure, Secondary
  • Saccharomyces cerevisiae Proteins
  • Saccharomycetales
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Identity

PubMed Central ID

  • PMC4832064

International Standard Serial Number (ISSN)

  • 2041-1723

Digital Object Identifier (DOI)

  • 10.1038/ncomms11265

PubMed ID

  • 27068241
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Additional Document Info

volume

  • 7

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