TORC2-Gad8 dependent myosin phosphorylation modulates regulation by calcium

  1. Karen Baker
  2. Irene A Gyamfi
  3. Gregory I Mashanov
  4. Justin E Molloy
  5. Michael A Geeves
  6. Daniel P Mulvihill  Is a corresponding author
  1. University of Kent, United Kingdom
  2. The Francis Crick Institute, United Kingdom

Abstract

Cells respond to changes in their environment through signalling networks that modulate cytoskeleton and membrane organisation to coordinate cell cycle progression, polarised cell growth and multicellular development. Here, we define a novel regulatory mechanism by which the motor activity and function of the fission yeast type 1 myosin, Myo1, is modulated by TORC2 signalling dependent phosphorylation. Phosphorylation of the conserved serine at position 742 within the neck region changes both the conformation of the neck region and the interactions between Myo1 and its associating calmodulin light chains. S742 phosphorylation thereby couples calcium and TOR signalling networks in the modulation of myosin-1 dynamics to co-ordinate actin polymerisation and membrane reorganisation at sites of endocytosis and polarised cell growth in response to environmental and cell cycle cues.

Data availability

Raw data files for Figures and Tables, and data analysis spreadsheets, are uploaded onto the University of Kent Data Repository server and are available at the following location: https://data.kent.ac.uk/60/

The following data sets were generated

Article and author information

Author details

  1. Karen Baker

    School of Biosciences, University of Kent, Canterbury, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  2. Irene A Gyamfi

    School of Biosciences, University of Kent, Canterbury, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  3. Gregory I Mashanov

    The Francis Crick Institute, London, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
  4. Justin E Molloy

    The Francis Crick Institute, London, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-8307-2450
  5. Michael A Geeves

    School of Biosciences, University of Kent, Canterbury, United Kingdom
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-9364-8898
  6. Daniel P Mulvihill

    School of Biosciences, University of Kent, Canterbury, United Kingdom
    For correspondence
    D.P.Mulvihill@kent.ac.uk
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0003-2502-5274

Funding

Biotechnology and Biological Sciences Research Council (BB/J012793/1)

  • Michael A Geeves
  • Daniel P Mulvihill

Biotechnology and Biological Sciences Research Council (BB/M015130/1)

  • Irene A Gyamfi
  • Daniel P Mulvihill

Royal Society (Industry Fellowship)

  • Daniel P Mulvihill

Cancer Research UK (FC001119)

  • Gregory I Mashanov
  • Justin E Molloy

Medical Research Council (FC001119)

  • Gregory I Mashanov
  • Justin E Molloy

Wellcome (FC001119)

  • Gregory I Mashanov
  • Justin E Molloy

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Copyright

© 2019, Baker et al.

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.

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  1. Karen Baker
  2. Irene A Gyamfi
  3. Gregory I Mashanov
  4. Justin E Molloy
  5. Michael A Geeves
  6. Daniel P Mulvihill
(2019)
TORC2-Gad8 dependent myosin phosphorylation modulates regulation by calcium
eLife 8:e51150.
https://doi.org/10.7554/eLife.51150

Share this article

https://doi.org/10.7554/eLife.51150

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