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Mechanism of the translocation of endcpinsmic reticulum by myosin XI in higher plant cells

高等植物细胞中肌球蛋白XI对端粒网的易位机制

基本信息

批准号：
17570043
负责人：
YOKOTA Etsuo
金额：
$ 2.3万
依托单位：
University of Hyogo
依托单位国家：
日本
项目类别：
Grant-in-Aid for Scientific Research (C)
财政年份：
2005
资助国家：
日本
起止时间：
2005 至 2006
项目状态：
已结题

来源：
https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-17570043/
关键词：
myosin XI 175-kDa myosin endonlasmic reticulum Network structure in vitro motility assay GTP actin tobacco cultured cell, BY-2 原形質流動運動再構成系小胞体チューブ構造ミオシン細胞周期フラグモプラスト

项目摘要

In tobacco cultured cells, BY-Z an isoform of myosin X, 175-kDa myosin, which is composed of 175-kDa heavy chain, is believed to be involved in the translocation of endoplasmic reticulum (ER). To further examine the relation of this myosin with ER translocation, cell fractionation procedure was carried out by using BY-2 TM cells expressing GFP-labeled ER (GFP-ER). Both 175-kDa myosin and GFP-ER, were detected in microsomal and cytosolic fractions prepared by the centrifugation. When these fractions were further fractioned by the sucrose-densityOgradient centrifugation, one portion of 175-kDa myosin was co-fractionated with GFP-ER, indicating that this myosin was tightly associated with ER and responsible for its translocation. In in vitro motility assay however, such ER associated with 175-kDa myosin was nor able to move along actin bundles in Chara internodal cells even in the presence of ATP. Interestingly, tubular structures were formed from vesicles of GFP-ER when GTP was added. These structures were considered to correspond to the tubular structures of ER observed in the cortical regions in living cells. However, the addition of other nucleotides such as GDP or ATP, instead of GTP, were not able to assemble the tubular structures of ER. Same phenomenon has been documented in the ER fraction prepared from Xenopus eggs. However, in the case of GFP-ER from BY-2 cells, the force such as stream was necessary to induce the elongation of tubular structures of ER in vitro. The elongation and shrinking of ER tubes in living BY-2 cells was significantly suppressed by inhibitors for actin cytoskeleton, but not for microtuble cytoskeleton. Hence, the force needed for the ER-tube elongation in vivo was suggested to be generated by actin cytoskeleton, especially molecular motor, myosin.

在烟草培养细胞中，肌球蛋白X的一个亚型，即175 kDa的肌球蛋白，被认为参与了内质网(ER)的转运。为了进一步研究这种肌球蛋白与内质网易位的关系，用表达GFP标记ER(GFP-ER)的BY-2 TM细胞进行了细胞分离。在离心法制备的微粒体组分和胞质组分中均检测到175 kDa的肌球蛋白和GFP-ER。当用蔗糖密度梯度离心法进一步分离这些组分时，175 kDa肌球蛋白的一部分与GFP-ER共分级，表明该肌球蛋白与内质网密切相关，并与其易位有关。然而，在体外运动分析中，这种与175 kDa肌球蛋白相关的内质网即使在ATP存在的情况下也不能沿着轮状结间细胞的肌动蛋白束移动。有趣的是，当加入GTP时，GFP-ER的囊泡形成了管状结构。这些结构被认为与在活细胞的皮质区域观察到的内质网管状结构相对应。然而，添加其他核苷酸如GDP或ATP，而不是GTP，不能组装内质网的管状结构。同样的现象也被记录在从非洲爪哇卵中提取的ER组分中。然而，对于来自BY-2细胞的GFP-ER，在体外诱导ER的管状结构延长是必要的力，如STREAM。肌动蛋白细胞骨架抑制剂能显著抑制BY-2细胞内ER管的伸长和收缩，但对微管细胞骨架的抑制作用不明显。因此，肌动蛋白细胞骨架，特别是分子马达，肌球蛋白，可能是肌动蛋白在体内延长ER管所需的力。

项目成果

期刊论文数量（16）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

Microtubule- and actin filament-dependent motors are distributed on pollen tube mitochondria and contribute differently to their movement

DOI：
10.1093/pcp/pcm001
发表时间：
2007-02-01
期刊：
PLANT AND CELL PHYSIOLOGY
影响因子：
4.9
作者：
Romagnoli, Silvia;Cai, Giampiero;Cresti, Mauro
通讯作者：
Cresti, Mauro

Plant villin, lily P-135-ABP, possesses the binding activity to G-actin and accelerates polymerization and depolymerization of actin in a Ca^<2+>-sensitive manner.

植物绒毛，百合P-135-ABP，具有与G-肌动蛋白的结合活性，并以Ca 2- 敏感的方式加速肌动蛋白的聚合和解聚。

DOI：
发表时间：
2005
期刊：
Plant and Cell Physiology 46
影响因子：
0
作者：
Kumatani;T.;K.Hashimoto;E.Yokota
通讯作者：
E.Yokota

Possible association of actin filaments with chloroplasts of spinach mesophyll in vivo and invitro.

体内和体外肌动蛋白丝与菠菜叶肉叶绿体的可能关联。

DOI：
发表时间：
2006
期刊：
Protoplasma 229
影响因子：
0
作者：
Kumatani;T.
通讯作者：
T.

Plant villin, lily P-135-ABP, possesses G-actin binding activity and accelerates the polymerization and depolymerization of actin in a Ca2+-sensitive manner.

DOI：
10.1093/pcp/pci185
发表时间：
2005-10
期刊：
Plant & cell physiology
影响因子：
4.9
作者：
E. Yokota;M. Tominaga;I. Mabuchi;Yasunori Tsuji;C. Staiger;K. Oiwa;T. Shimmen
通讯作者：
E. Yokota;M. Tominaga;I. Mabuchi;Yasunori Tsuji;C. Staiger;K. Oiwa;T. Shimmen

Peroxisomal localization of myosin XI isoform in Arabidopsis thaliana.

拟南芥中肌球蛋白 XI 亚型的过氧化物酶体定位。