期刊
CURRENT BIOLOGY
卷 24, 期 5, 页码 579-585出版社
CELL PRESS
DOI: 10.1016/j.cub.2014.01.072
关键词
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资金
- NIH [R01 GM079265]
- ACS [RSG-11-126-01-CSM, IRG-1105201]
- NIH MCB Training Grant [T32 GM0071832]
- AHA [11SDG5470024]
Controlling the quantity and size of organelles through competition for a limited supply of components is quickly emerging as an important cellular regulatory mechanism [1]. Cells assemble diverse actin filament (F-actin) networks for fundamental processes including division, motility, and polarization [2-4]. F-actin polymerization is tightly regulated by activation of assembly factors such as the Arp2/3 complex and formins at specific times and places. We directly tested an additional hypothesis that diverse F-actin networks are in homeostasis, whereby competition for actin monomers (G-actin) is critical for regulating F-actin network size. Here we show that inhibition of Arp2/3 complex in the fission yeast Schizosaccharomyces pombe not only depletes Arp2/3-complex-mediated endocytic actin patches, but also induces a dramatic excess of formin-assembled F-actin. Conversely, disruption of formin increases the density of Arp2/3-complex-mediated patches. Furthermore, modification of actin levels significantly perturbs the fission yeast actin cytoskeleton. Increasing actin favors Arp2/3-complex-mediated actin assembly, whereas decreasing actin favors formin-mediated contractile rings. Therefore, the specific actin concentration in a cell is critical, and competition for G-actin helps regulate the proper amount of F-actin assembly for diverse processes.
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