Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis
Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis
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DOI：
10.1016/s1534-5807(03)00324-1
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发表时间：
2003-11-01
影响因子：
11.8
通讯作者：
Pollard, TD
中科院分区：
文献类型：
--
作者：
Wu, JQ;Kuhn, JR;Pollard, TD
荧光融合蛋白和遗传相关性的显微镜观察表明，分裂酵母以精确的时间顺序组装和收缩细胞动力收缩环。在纺锤体极体(SPB)分离前90分钟，类苯胺素蛋白[Mid1p]从细胞核迁移，并将赤道周围的一条宽带皮质指定为分裂位置。在SPB分离前10分钟至分离后2分钟，常规肌球蛋白-II(Myo2p)、IQGAP(Rng2p)、PCH蛋白(CDc15p)和Forin(CDc12p)加入不依赖肌动蛋白细丝的宽带。在后期B之前的10分钟内，这条宽阔的蛋白质带浓缩成一个收缩环，包括肌动蛋白、原肌球蛋白(Cdc8p)和α-肌动蛋白(Ain1p)。在B后期，非常规肌球蛋白-II(Myp2p)加入环，随后是Septin(Spn1p)。SPB分离后37分钟开始环收缩和解体。这种空间和时间层次为分析分子机制提供了框架。
Microscopy of fluorescent fusion proteins and genetic dependencies show that fission yeast assemble and constrict a cytokinetic contractile ring in a precisely timed, sequential order. More than 90 min prior to separation of the spindle pole bodies (SPB), the anillin-like protein [Mid1p) migrates from the nucleus and specifies a broad band of cortex around the equator as the division site. Between 10 min before and 2 min after SPB separation, conventional myosin-II (Myo2p), IQGAP (Rng2p), PCH protein (Cdc15p), and formin (Cdc12p) join the broad band independent of actin filaments. Over the subsequent 10 min prior to anaphase B, this broad band of proteins condenses into a contractile ring including actin, tropomyosin (Cdc8p), and alpha-actinin (Ain1p). During anaphase B, unconventional myosin-II (Myp2p) joins the ring followed by the septin (Spn1p). Ring contraction and disassembly begin 37 min after SPB separation. This spatial and temporal hierarchy provides the framework for analysis of molecular mechanisms.