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.
Article and author information
Author details
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.
Reviewing Editor
- Pekka Lappalainen, University of Helsinki, Finland
Publication history
- Received: August 16, 2019
- Accepted: September 26, 2019
- Accepted Manuscript published: September 30, 2019 (version 1)
- Version of Record published: October 21, 2019 (version 2)
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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