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本文引用的文献

1
hnRNP I is required to generate the Ca2+ signal that causes egg activation in zebrafish.异质性核糖核蛋白I是产生导致斑马鱼卵子激活的钙离子信号所必需的。
Development. 2009 Sep;136(17):3007-17. doi: 10.1242/dev.037879.
2
KDP-1 is a nuclear envelope KASH protein required for cell-cycle progression.KDP-1是细胞周期进程所必需的一种核膜KASH蛋白。
J Cell Sci. 2009 Aug 15;122(Pt 16):2895-905. doi: 10.1242/jcs.051607. Epub 2009 Jul 28.
3
A ZYG-12-dynein interaction at the nuclear envelope defines cytoskeletal architecture in the C. elegans gonad.核膜处的ZYG-12与动力蛋白的相互作用决定了秀丽隐杆线虫性腺中的细胞骨架结构。
J Cell Biol. 2009 Jul 27;186(2):229-41. doi: 10.1083/jcb.200902101.
4
UNC-83 is a nuclear-specific cargo adaptor for kinesin-1-mediated nuclear migration.UNC-83是一种用于驱动蛋白-1介导的核迁移的核特异性货物衔接蛋白。
Development. 2009 Aug;136(16):2725-33. doi: 10.1242/dev.038596. Epub 2009 Jul 15.
5
Kinesin-1 and cytoplasmic dynein act sequentially to move the meiotic spindle to the oocyte cortex in Caenorhabditis elegans.在秀丽隐杆线虫中,驱动蛋白-1和细胞质动力蛋白依次作用,将减数分裂纺锤体移动到卵母细胞皮层。
Mol Biol Cell. 2009 Jun;20(11):2722-30. doi: 10.1091/mbc.e08-12-1253. Epub 2009 Apr 8.
6
NuMA-related LIN-5, ASPM-1, calmodulin and dynein promote meiotic spindle rotation independently of cortical LIN-5/GPR/Galpha.与核有丝分裂器蛋白相关的LIN-5、ASPM-1、钙调蛋白和动力蛋白可独立于皮层LIN-5/GPR/Gα促进减数分裂纺锤体旋转。
Nat Cell Biol. 2009 Mar;11(3):269-77. doi: 10.1038/ncb1834. Epub 2009 Feb 15.
7
Rab11 is required for synchronous secretion of chondroitin proteoglycans after fertilization in Caenorhabditis elegans.秀丽隐杆线虫受精后,软骨素蛋白聚糖的同步分泌需要Rab11。
J Cell Sci. 2008 Oct 1;121(Pt 19):3177-86. doi: 10.1242/jcs.034678. Epub 2008 Sep 2.
8
EGG-3 regulates cell-surface and cortex rearrangements during egg activation in Caenorhabditis elegans.EGG-3在秀丽隐杆线虫卵激活过程中调节细胞表面和皮层重排。
Curr Biol. 2007 Sep 18;17(18):1555-60. doi: 10.1016/j.cub.2007.08.011.
9
Caenorhabditis elegans SAND-1 is essential for RAB-7 function in endosomal traffic.秀丽隐杆线虫的SAND-1在内体运输中对RAB-7功能至关重要。
EMBO J. 2007 Jan 24;26(2):301-12. doi: 10.1038/sj.emboj.7601498. Epub 2007 Jan 4.
10
Katanin controls mitotic and meiotic spindle length.katanin蛋白控制有丝分裂和减数分裂纺锤体的长度。
J Cell Biol. 2006 Dec 18;175(6):881-91. doi: 10.1083/jcb.200608117.

依赖于驱动蛋白的运输导致卵母细胞中的核呈极化迁移,以及减数分裂胚胎中卵黄颗粒向内运动。

Kinesin-dependent transport results in polarized migration of the nucleus in oocytes and inward movement of yolk granules in meiotic embryos.

机构信息

Section of Molecular and Cellular Biology, 149 Briggs Hall, University of California, Davis, Davis, CA 95616, USA.

出版信息

Dev Biol. 2010 Mar 1;339(1):126-40. doi: 10.1016/j.ydbio.2009.12.021. Epub 2009 Dec 28.

DOI:10.1016/j.ydbio.2009.12.021
PMID:20036653
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2823969/
Abstract

During female meiosis, meiotic spindles are positioned at the oocyte cortex to allow expulsion of chromosomes into polar bodies. In C. elegans, kinesin-dependent translocation of the entire spindle to the cortex precedes dynein-dependent rotation of one spindle pole toward the cortex. To elucidate the role of kinesin-1 in spindle translocation, we examined the localization of kinesin subunits in meiotic embryos. Surprisingly, kinesin-1 was not associated with the spindle and instead was restricted to the cytoplasm in the middle of the embryo. Yolk granules moved on linear tracks, in a kinesin-dependent manner, away from the cortex, resulting in their concentration in the middle of the embryo where the kinesin was concentrated. These results suggest that cytoplasmic microtubules might be arranged with plus ends extending inward, away from the cortex. This microtubule arrangement would not be consistent with direct transport of the meiotic spindle toward the cortex by kinesin-1. In maturing oocytes, the nucleus underwent kinesin-dependent migration to the future site of spindle attachment at the anterior cortex. Thus the spindle translocation defect observed in kinesin-1 mutants may be a result of failed nuclear migration, which places the spindle too far from the cortex for the spindle translocation mechanism to function.

摘要

在雌性减数分裂过程中,减数分裂纺锤体定位于卵母细胞皮层,以允许染色体排出到极体中。在秀丽隐杆线虫中,整个纺锤体依赖于驱动蛋白的易位先于依赖于动力蛋白的一个纺锤体极向皮层的旋转。为了阐明驱动蛋白-1在纺锤体易位中的作用,我们检查了减数分裂胚胎中驱动蛋白亚基的定位。令人惊讶的是,驱动蛋白-1与纺锤体无关,而是局限于胚胎中部的细胞质中。卵黄颗粒以依赖于驱动蛋白的方式在线性轨道上移动,远离皮层,导致它们在细胞质中浓缩,而细胞质中的驱动蛋白也集中于此。这些结果表明,细胞质微管可能以向外延伸的正端排列,远离皮层。这种微管排列与驱动蛋白-1直接将减数分裂纺锤体向皮层运输不一致。在成熟的卵母细胞中,核经历了驱动蛋白依赖性的迁移,以到达前皮层纺锤体附着的未来位置。因此,在驱动蛋白-1突变体中观察到的纺锤体易位缺陷可能是核迁移失败的结果,这使得纺锤体离皮层太远,无法使纺锤体易位机制发挥作用。