%0 Journal Article %1 yang2012arp23 %A Yang, Qing %A Zhang, Xiao-Feng %A Pollard, Thomas D. %A Forscher, Paul %D 2012 %J The Journal of Cell Biology %K actin arp23 cell mechanism migration phd %N 7 %P 939-956 %R 10.1083/jcb.201111052 %T Arp2/3 complex–dependent actin networks constrain myosin II function in driving retrograde actin flow %U http://jcb.rupress.org/content/197/7/939.abstract %V 197 %X The Arp2/3 complex nucleates actin filaments to generate networks at the leading edge of motile cells. Nonmuscle myosin II produces contractile forces involved in driving actin network translocation. We inhibited the Arp2/3 complex and/or myosin II with small molecules to investigate their respective functions in neuronal growth cone actin dynamics. Inhibition of the Arp2/3 complex with CK666 reduced barbed end actin assembly site density at the leading edge, disrupted actin veils, and resulted in veil retraction. Strikingly, retrograde actin flow rates increased with Arp2/3 complex inhibition; however, when myosin II activity was blocked, Arp2/3 complex inhibition now resulted in slowing of retrograde actin flow and veils no longer retracted. Retrograde flow rate increases induced by Arp2/3 complex inhibition were independent of Rho kinase activity. These results provide evidence that, although the Arp2/3 complex and myosin II are spatially segregated, actin networks assembled by the Arp2/3 complex can restrict myosin II–dependent contractility with consequent effects on growth cone motility.

@article{yang2012arp23, abstract = {The Arp2/3 complex nucleates actin filaments to generate networks at the leading edge of motile cells. Nonmuscle myosin II produces contractile forces involved in driving actin network translocation. We inhibited the Arp2/3 complex and/or myosin II with small molecules to investigate their respective functions in neuronal growth cone actin dynamics. Inhibition of the Arp2/3 complex with CK666 reduced barbed end actin assembly site density at the leading edge, disrupted actin veils, and resulted in veil retraction. Strikingly, retrograde actin flow rates increased with Arp2/3 complex inhibition; however, when myosin II activity was blocked, Arp2/3 complex inhibition now resulted in slowing of retrograde actin flow and veils no longer retracted. Retrograde flow rate increases induced by Arp2/3 complex inhibition were independent of Rho kinase activity. These results provide evidence that, although the Arp2/3 complex and myosin II are spatially segregated, actin networks assembled by the Arp2/3 complex can restrict myosin II–dependent contractility with consequent effects on growth cone motility.}, added-at = {2014-06-04T10:13:05.000+0200}, author = {Yang, Qing and Zhang, Xiao-Feng and Pollard, Thomas D. and Forscher, Paul}, biburl = {https://www.bibsonomy.org/bibtex/2c53f35063a7c027df5118367c474113c/bkoch}, description = {Arp2/3 complex–dependent actin networks constrain myosin II function in driving retrograde actin flow}, doi = {10.1083/jcb.201111052}, eprint = {http://jcb.rupress.org/content/197/7/939.full.pdf+html}, interhash = {057f2d94c35694a326c1583ce9f437de}, intrahash = {c53f35063a7c027df5118367c474113c}, journal = {The Journal of Cell Biology}, keywords = {actin arp23 cell mechanism migration phd}, number = 7, pages = {939-956}, timestamp = {2014-06-04T10:13:05.000+0200}, title = {Arp2/3 complex–dependent actin networks constrain myosin II function in driving retrograde actin flow}, url = {http://jcb.rupress.org/content/197/7/939.abstract}, volume = 197, year = 2012 }