2015
DOI: 10.1038/ncomms7297
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Activity-driven relaxation of the cortical actomyosin II network synchronizes Munc18-1-dependent neurosecretory vesicle docking

Abstract: In neurosecretory cells, secretory vesicles (SVs) undergo Ca 2 þ -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 th… Show more

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Cited by 61 publications
(87 citation statements)
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“…Nanoscissor-induced sudden release of cortical actin tension results in quick recoil of the plasma membrane proximal to the incision point indicating that the actomyosin cortex controls plasma membrane tension (Papadopulos et al, 2015). This effect could not be seen upon pre-treatment with myosin II inhibitor blebbistatin strongly suggesting that the cortical tension mainly depend on actomyosin II activity.…”
Section: Accepted Manuscriptmentioning
confidence: 74%
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“…Nanoscissor-induced sudden release of cortical actin tension results in quick recoil of the plasma membrane proximal to the incision point indicating that the actomyosin cortex controls plasma membrane tension (Papadopulos et al, 2015). This effect could not be seen upon pre-treatment with myosin II inhibitor blebbistatin strongly suggesting that the cortical tension mainly depend on actomyosin II activity.…”
Section: Accepted Manuscriptmentioning
confidence: 74%
“…Over time this picture become more complex and dynamic ( Fig. 1), with evidence that the cortical actin network is involved in (i) tethering secretory vesicles (Aschenbrenner et al, 2003;Au et al, 2007;Chibalina et al, 2007;Desnos et al, 2007;Huet et al, 2012;Tomatis et al, 2013), (ii) providing a platform for directed movement towards the plasma membrane (Papadopulos et al, 2015) and (iii) facilitating the generation of new release sites (de Paiva et al, 1999;Zakharenko et al, 1999).…”
Section: +mentioning
confidence: 99%
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“…Inhibition of the RhoA-ROCK pathway might favor the SNARE complex formation by preventing tomosyn/syntaxin-1 interaction. Alternatively, it might regulate the level of myosin light chain (MLC) phosphorylation and therefore modulate the myosin-induced forces required for exocytosis [32] . These two hypotheses are not mutually exclusive and required further investigations.…”
Section: Oligophrenin-1 a New Actor In Calcium-regulated Exocytosismentioning
confidence: 99%