TORC2-Gad8 dependent myosin phosphorylation modulates regulation by calcium
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.
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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/
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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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