Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis.
Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis.
复制标题
计算收缩环中的肌动蛋白揭示了cofilin和II型肌球蛋白对分裂酵母细胞分裂的新贡献。
DOI:
10.1091/mbc.e21-08-0376
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发表时间:
2022-05-15
影响因子:
3.3
通讯作者:
Chen, Qian
中科院分区:
文献类型:
--
作者:
Malla, Mamata;Pollard, Thomas D.;Chen, Qian
Cytokinesis by animals, fungi, and amoebas depends on actomyosin contractile rings, which are stabilized by continuous turnover of actin filaments. Remarkably little is known about the amount of polymerized actin in contractile rings, so we used low concentrations of GFP-Lifeact to count total polymerized actin molecules in the contractile rings of live fission yeast cells. Contractile rings of wild-type cells accumulated polymerized actin molecules at 4900/min to a peak number of ∼198,000 followed by a loss of actin at 5400/min throughout ring constriction. In adf1-M3 mutant cells with cofilin that severs actin filaments poorly, contractile rings accumulated polymerized actin at twice the normal rate and eventually had almost twofold more actin along with a proportional increase in type II myosins Myo2, Myp2, and formin Cdc12. Although 30% of adf1-M3 mutant cells failed to constrict their rings fully, the rest lost actin from the rings at the wild-type rates. Mutations of type II myosins Myo2 and Myp2 reduced contractile ring actin filaments by half and slowed the rate of actin loss from the rings.
DOI:
10.1083/jcb.146.2.453
发表时间:
1999-07-26
期刊:
The Journal of cell biology
影响因子:
--
作者:
Konzok A;Weber I;Simmeth E;Hacker U;Maniak M;Müller-Taubenberger A
通讯作者:
Müller-Taubenberger A