The Francis Crick Institute
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TORC2-Gad8-dependent myosin phosphorylation modulates regulation by calcium.

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journal contribution
posted on 2020-01-17, 13:59 authored by Karen Baker, Irene A Gyamfi, Gregory I Mashanov, Justin E Molloy, Michael A Geeves, Daniel P Mulvihill
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.


Crick (Grant ID: 10119, Grant title: Molloy FC001119)