Key result
TORC2-dependent phosphorylation of a conserved serine in the neck region of fission yeast myosin-1 modulates its interaction with calmodulins and promotes calcium-dependent switching between light chains to regulate endocytosis.
This basic science study reveals a novel mechanism by which TORC2-dependent myosin neck phosphorylation modulates acto-myosin dynamics to control polarized cell growth in fission yeast.
No immediate clinical implications; leaves open conserved myosin regulation in mammalian systems.
All cells have the ability to respond to changes in their environment. Signalling networks modulate cytoskeleton and membrane organisation to impact cell cycle progression, polarised cell growth and multicellular development according to the environmental setting. Using diverse in vitro, in vivo and single molecule techniques we have explored the role of myosin-1 signalling in regulating endocytosis during both mitotic and meiotic cell cycles. We have established that a conserved serine within the neck region of the sole fission yeast myosin-1 is phosphorylated in a TORC2 dependent manner to modulate myosin function. Myo1 neck phosphorylation brings about a change in the conformation of the neck region and modifies its interaction with calmodulins, Myo1 dynamics at endocytic foci, and promotes calcium dependent switching between different calmodulin light chains. These data provide insight into a novel mechanism by which myosin neck phosphorylation modulates acto-myosin dynamics to control polarised cell growth in response to mitotic and meiotic cell-cycle progression and the cellular environment.
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Baker et al. (2018) studied this question. Myo1S742 phosphorylation / myo1.S742A mutation vs. Wild type Myo1 was evaluated on Myo1 and calmodulin dynamics during endocytosis. TORC2-dependent phosphorylation of a conserved serine in the neck region of fission yeast myosin-1 modulates its interaction with calmodulins and promotes calcium-dependent switching between light chains to regulate endocytosis.
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