Evidence for F-actin-dependent and -independent mechanisms involved in assembly and stability of the medial actomyosin ring in fission yeast

被引:109
作者
Naqvi, NI
Eng, K
Gould, KL
Balasubramanian, MK
机构
[1] Natl Univ Singapore, Inst Mol Agrobiol, Cell Div Lab, Singapore 117604, Singapore
[2] Vanderbilt Univ, Sch Med, Howard Hughes Med Inst, Nashville, TN 37232 USA
[3] Vanderbilt Univ, Sch Med, Dept Cell Biol, Nashville, TN 37232 USA
关键词
Cdc4p; cytokinesis; Myo2p; myosin II; S-pombe;
D O I
10.1093/emboj/18.4.854
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cell division in a number of eukaryotes, including the fission yeast Schizosaccharomyces pombe, is achieved through a medially placed actomyosin-based contractile ring. Although several components of the actomyosin ring have been identified, the mechanisms regulating ring assembly are still not understood. Here, we show by biochemical and mutational studies that the S.pombe actomyosin ring component Cdc4p is a light chain associated with Myo2p, a myosin II heavy chain, Localization of Myo2p to the medial ring depended on Cdc4p function, whereas localization of Cdc4p at the division site was independent of Myo2p, Interestingly, the actin-binding and motor domains of Myo2p are not required for its accumulation at the division site although the motor activity of Myo2p is essential for assembly of a normal actomyosin ring, The initial assembly of Myo2p and Cdc4p at the division site requires a functional F-actin cytoskeleton, Once established, however, P-actin is not required for the maintenance of Cdc4p and Myo2p medial rings, suggesting that the attachment of Cdc4p and Myo2p to the division site involves proteins other than actin itself.
引用
收藏
页码:854 / 862
页数:9
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