• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>Cell Regulation >Dephosphorylation of Major Sperm Protein (MSP) Fiber Protein 3 by Protein Phosphatase 2A during Cell Body Retraction in the MSP-based Amoeboid Motility of Ascaris Sperm
【2h】

Dephosphorylation of Major Sperm Protein (MSP) Fiber Protein 3 by Protein Phosphatase 2A during Cell Body Retraction in the MSP-based Amoeboid Motility of Ascaris Sperm

机译：在A虫精子的基于MSP的变形虫运动中细胞主体缩回过程中蛋白磷酸酶2A对主要精子蛋白（MSP）纤维蛋白3的去磷酸化作用

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The crawling movement of nematode sperm requires coordination of leading edge protrusion with cell body retraction, both of which are powered by modulation of a cytoskeleton based on major sperm protein (MSP) filaments. We used a cell-free in vitro motility system in which both protrusion and retraction can be reconstituted, to identify two proteins involved in cell body retraction. Pharmacological and depletion-add back assays showed that retraction was triggered by a putative protein phosphatase 2A (PP2A, a Ser/Thr phosphatase activated by tyrosine dephosphorylation). Immunofluorescence showed that PP2A was present in the cell body and was concentrated at the base of the lamellipod where the force for retraction is generated. PP2A targeted MSP fiber protein 3 (MFP3), a protein unique to nematode sperm that binds to the MSP filaments in the motility apparatus. Dephosphorylation of MFP3 caused its release from the cytoskeleton and generated filament disassembly. Our results suggest that interaction between PP2A and MFP3 leads to local disassembly of the MSP cytoskeleton at the base of the lamellipod in sperm that in turn pulls the trailing cell body forward.
机译：线虫精子的爬行运动需要使前缘突起与细胞主体缩回协调，这两者都由基于主要精子蛋白（MSP）细丝的细胞骨架的调节提供动力。我们使用了一种无细胞的体外运动系统，在该系统中可以重构突出和缩回，以鉴定参与细胞体缩回的两种蛋白质。药理和耗竭回加分析表明，撤回是由推定的蛋白磷酸酶2A（PP2A，酪氨酸脱磷酸激活的Ser / Thr磷酸酶）触发的。免疫荧光显示PP2A存在于细胞体内，并集中在产生回缩力的lamellipod的底部。 PP2A靶向MSP纤维蛋白3（MFP3），这是线虫精子特有的蛋白，可与运动装置中的MSP细丝结合。 MFP3的去磷酸化导致其从细胞骨架释放，并产生细丝分解。我们的结果表明，PP2A和MFP3之间的相互作用导致精子中lamellipod底部的MSP细胞骨架局部解体，进而将尾随的细胞体向前拉。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号