Myosin II functions in actin-bundle turnover in neuronal growth cones

2006 ◽  
Vol 8 (3) ◽  
pp. 216-226 ◽  
Author(s):  
Nelson A. Medeiros ◽  
Dylan T. Burnette ◽  
Paul Forscher

2013 ◽  
Vol 24 (19) ◽  
pp. 3097-3114 ◽  
Author(s):  
Qing Yang ◽  
Xiao-Feng Zhang ◽  
David Van Goor ◽  
Ashleigh P. Dunn ◽  
Callen Hyland ◽  
...  

Protein kinase C (PKC) can dramatically alter cell structure and motility via effects on actin filament networks. In neurons, PKC activation has been implicated in repulsive guidance responses and inhibition of axon regeneration; however, the cytoskeletal mechanisms underlying these effects are not well understood. Here we investigate the acute effects of PKC activation on actin network structure and dynamics in large Aplysia neuronal growth cones. We provide evidence of a novel two-tiered mechanism of PKC action: 1) PKC activity enhances myosin II regulatory light chain phosphorylation and C-kinase–potentiated protein phosphatase inhibitor phosphorylation. These effects are correlated with increased contractility in the central cytoplasmic domain. 2) PKC activation results in significant reduction of P-domain actin network density accompanied by Arp2/3 complex delocalization from the leading edge and increased rates of retrograde actin network flow. Our results show that PKC activation strongly affects both actin polymerization and myosin II contractility. This synergistic mode of action is relevant to understanding the pleiotropic reported effects of PKC on neuronal growth and regeneration.



2021 ◽  
Vol 120 (3) ◽  
pp. 170a
Author(s):  
Kahmina R. Ford ◽  
Erin M. Craig


2003 ◽  
Vol 57 (1) ◽  
pp. 31-37 ◽  
Author(s):  
Erika M. A. Negreiros ◽  
Ana C. M. Leão ◽  
Marcelo F. Santiago ◽  
Rosalia Mendez-Otero








2000 ◽  
Vol 20 (4) ◽  
pp. 1484-1494 ◽  
Author(s):  
Thomas J. Diefenbach ◽  
Peter B. Guthrie ◽  
Stanley B. Kater






2014 ◽  
Vol 106 (2) ◽  
pp. 357a
Author(s):  
Mikael Garcia ◽  
Cécile Leduc ◽  
Amélie Argento ◽  
Jean-Baptiste Sibarita ◽  
Olivier R. Thoumine


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