Activity-driven relaxation of the cortical actomyosin II network synchronizes Munc18-1-dependent neurosecretory vesicle docking

Andreas Papadopulos (), Guillermo A. Gomez, Sally Martin, Jade Jackson, Rachel S. Gormal, Damien J. Keating, Alpha S. Yap and Frederic A. Meunier ()
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Andreas Papadopulos: The Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland
Guillermo A. Gomez: The University of Queensland
Sally Martin: The Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland
Jade Jackson: Molecular and Cellular Neuroscience Laboratory, Flinders University
Rachel S. Gormal: The Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland
Damien J. Keating: Molecular and Cellular Neuroscience Laboratory, Flinders University
Alpha S. Yap: The University of Queensland
Frederic A. Meunier: The Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: Abstract In neurosecretory cells, secretory vesicles (SVs) undergo Ca2+-dependent fusion with the plasma membrane to release neurotransmitters. How SVs cross the dense mesh of the cortical actin network to reach the plasma membrane remains unclear. Here we reveal that, in bovine chromaffin cells, SVs embedded in the cortical actin network undergo a highly synchronized transition towards the plasma membrane and Munc18-1-dependent docking in response to secretagogues. This movement coincides with a translocation of the cortical actin network in the same direction. Both effects are abolished by the knockdown or the pharmacological inhibition of myosin II, suggesting changes in actomyosin-generated forces across the cell cortex. Indeed, we report a reduction in cortical actin network tension elicited on secretagogue stimulation that is sensitive to myosin II inhibition. We reveal that the cortical actin network acts as a ‘casting net’ that undergoes activity-dependent relaxation, thereby driving tethered SVs towards the plasma membrane where they undergo Munc18-1-dependent docking.

Date: 2015
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DOI: 10.1038/ncomms7297

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