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首页> 外文期刊>Cell motility and the cytoskeleton >A critical role for the type V myosin, Myo52, in septum deposition and cell fission during cytokinesis in Schizosaccharomyces pombe.
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A critical role for the type V myosin, Myo52, in septum deposition and cell fission during cytokinesis in Schizosaccharomyces pombe.

机译：V型肌球蛋白Myo52在粟酒裂殖酵母的胞质分裂过程中在隔膜沉积和细胞分裂中的关键作用。

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摘要

Cytokinesis in fission yeast involves the coordination of septum deposition with the contraction of a cytokinetic actomyosin ring. We have examined the role of the type V myosin Myo52 in the coupling of these two events by the construction of a series of deletion mutants of the Myo52 tail and a further mutant within the ATP binding domain of the head. Each mutant protein was ectopically expressed in fission yeast cells. Each truncation was assayed for the ability to localize to the cell poles and septum (the normal cellular locations of Myo52) and to rescue the morphology defects and temperature sensitivity of a myo52Delta strain. A region within the Myo52 tail (amino acids 1320-1503), with a high degree of similarity to the vesicle-binding domain of the budding yeast type V myosin Myo2p, was essential for Myo52's role in the maintenance of growth polarity and cell division. A separate region (amino acids 1180-1320) was required for Myo52 foci to move throughout the cytoplasm; however, constructs lacking this region, but which retained the ability to dimerize still associated with actin at sites of cell growth. Not all of the Myo52 truncations which localized rescued the morphological defects of myo52Delta, demonstrating that loss of function was not simply brought about by an inability of mutant proteins to target the correct cellular location. By contrast, Myo52 motor activity was required for both localization and cellular function. myo52Delta cells were unable to efficiently localize the beta-1,3-glucan synthase, Bgs1, either at the cell poles or at the division septum, regions of cell wall deposition. Bgs1 and Myo52 localized to vesicle-like dots at the poles in interphase and these moved together to the septum at division. These data have led to the formulation of a model in which Myo52 is responsible for the delivery of Bgs1 and associated molecules to polar cell growth regions during interphase. On the commencement of septum formation, Myo52 transports Bgs1 to the cell equator, thus ensuring the accurate deposition of beta-1,3-glucan at the leading edge of the primary septum.
机译：裂变酵母中的胞质分裂涉及隔膜沉积与细胞动力学放线菌素环的收缩的协调。我们通过构建一系列Myo52尾巴的缺失突变体和头部ATP结合域内的另一个突变体，研究了V型肌球蛋白Myo52在这两个事件的偶联中的作用。每个突变蛋白在裂变酵母细胞中异位表达。测定每个截短的定位于细胞极和隔膜（Myo52的正常细胞位置）以及挽救myo52Delta菌株的形态缺陷和温度敏感性的能力。 Myo52尾部的一个区域（氨基酸1320-1503）与发芽的酵母V型肌球蛋白Myo2p的囊泡结合域高度相似，对于Myo52在维持生长极性和细胞分裂中的作用至关重要。 Myo52病灶需要一个单独的区域（氨基酸1180至1320）才能移动到整个细胞质中。然而，构建体缺乏该区域，但是保留了在细胞生长部位仍与肌动蛋白相关的二聚能力。并非所有定位于Myo52的截短都拯救了myo52Delta的形态缺陷，这表明功能丧失并非简单地由突变蛋白无法靶向正确的细胞位置引起。相比之下，Myo52运动活动是本地化和细胞功能所必需的。 myo52Delta细胞无法有效地定位β-1,3-葡聚糖合酶Bgs1，无论是在细胞极还是在隔壁处，都是细胞壁沉积的区域。 Bgs1和Myo52在相间的两极定位为囊泡状的点，并在分裂时一起移动到隔膜。这些数据导致了模型的建立，其中Myo52负责在相间将Bgs1和相关分子传递到极性细胞生长区域。在隔垫形成开始时，Myo52将Bgs1转运至细胞赤道，从而确保β-1,3-葡聚糖在主隔垫前缘的准确沉积。

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