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Actomyosin is Involved in the Organization of the Microtubule Preprophase Band in Arabidopsis Suspension Cultured Cells

Actomyosin is Involved in the Organization of the Microtubule Preprophase Band in Arabidopsis Suspension Cultured Cells

作     者:Chun-Li Li Zhi-Ling Chen Ming Yuan 

作者机构:State Key Laboratory of Plant Physiology and Biochemistry Department of Plant Sciences College of Biological Sciences China Agricultural University Beijing 100094 China College of Life Sciences Capital Normal University Beijing 100037 China 

出 版 物:《Journal of Integrative Plant Biology》 (植物学报(英文版))

年 卷 期:2006年第48卷第1期

页      面:53-61页

核心收录:

学科分类:0710[理学-生物学] 071001[理学-植物学] 07[理学] 

基  金:Supported by the State Key Basic Research and Development Plan of China (2006CB100101) and the National Natural Science Foundation of China (30421002  30370707 and 30100091 ) 

主  题:Arabidopsis suspension cultured cell 2,3-butanedine monoxime microfilament microtubule preprophase band myosin. 

摘      要:The microtubule preprophase bands (PPBs) participate in the sequence of events to position cell plates in most plants. However, the mechanism of PPB formation remains to be clarified. In the present study, the organization of PPBs in Arabidopsis suspension cultured cells was investigated by confocal laser scanning microscopy combined with pharmacological treatments of reagents specific for the cytoskeleton elements. Double staining of F-actin and microtubules (MTs) showed that actin filaments were arranged randomly and no colocalization with cortical MTs was observed in the interphase cells. However, cortical actin filaments showed colocalization with MTs during the formation of PPBs. A broad actin band formed with the broad MT band in the initiation of PPB and narrowed down together with the MT band to form the PPB. Nevertheless, broad MT bands were formed but failed to narrow down in cells treated with the F-actin disruptor latrunculin A. In contrast, in the presence of the F-actin stabilizer phalloidin, PPB formation did not exhibit any abnormality. Therefore, the integrity, but not the dynamics, of the actin cytoskeleton is necessary for the formation of normal PPBs. Treatment with 2, 3-butanedine monoxime, a myosin inhibitor, also resulted in the formation of broad MT bands, indicating that actomyosin may be involved in the rearrangement of MTs to form the PPBs. Double staining of MTs and myosin revealed that myosin concentrated on the PPB region during PPB formation. It is suggested that the actin cytoskeleton at the PPB site may serve as a rack to transport cortical MTs by using myosin when the broad MT band narrows down to form the PPB.

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