Regulation of Cytoplasmic Dynein

细胞质动力蛋白的调节

基本信息

  • 批准号:
    8630495
  • 负责人:
  • 金额:
    $ 48.66万
  • 依托单位:
  • 依托单位国家:
    美国
  • 项目类别:
  • 财政年份:
    2014
  • 资助国家:
    美国
  • 起止时间:
    2014-06-10 至 2018-02-28
  • 项目状态:
    已结题

项目摘要

PROJECT SUMMARY The long-term goal of this research project is to understand how the microtubule (MT)-based motor cytoplasmic dynein ("dynein") is regulated. Dynein is the largest and most complex of all cytoskeletal motors; this >1 MDa dimeric complex contains numerous mechanical elements whose movements must be coordinated over strikingly long molecular distances to achieve processive motility along MTs. In addition to its enormous size, dynein is also the most versatile of the molecular motors; in sharp contrast to the 45 kinesins and 39 myosins present in humans, a single dynein gene product is responsible for transporting macromolecules within neurons, constructing the mitotic spindle, polarizing cells, and anchoring mRNAs during development. To give dynein the functional plasticity necessary for carrying out its many roles, several ubiquitous co-factors interact with dynein, including Lis1 and the dynactin complex. This project will apply our combined expertise in biochemistry, single-molecule biophysics and cryo-electron microscopy to address the structural and mechanistic bases of dynein's interaction with MTs and its regulation by Lis1 and dynactin. We recently showed that binding of dynein to MTs is accompanied by conformational changes in its MT- binding domain and that Lis1 acts as a "clutch" to uncouple MT binding and release from ATP hydrolysis, promoting a strongly MT-attached state. Dynactin, a 1.2 MDa complex, enhances dynein's processivity and is required for nearly all dynein functions in cells, but its mechanism of action is poorly understood. This grant will address major mechanistic questions about dynein and its regulation. What are the structural and mechanistic bases of MT binding (Aim 1), and of regulation by Lis1 (Aim 2) and dynactin (Aim 3)?
项目总结

项目成果

期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)

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Andres Leschziner其他文献

Andres Leschziner的其他文献

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{{ truncateString('Andres Leschziner', 18)}}的其他基金

Mechanism of cytoskeletal transport and transcription-coupled DNA repair
细胞骨架运输和转录偶联DNA修复机制
  • 批准号:
    10405228
  • 财政年份:
    2022
  • 资助金额:
    $ 48.66万
  • 项目类别:
Mechanism of cytoskeletal transport and transcription-coupled DNA repair
细胞骨架运输和转录偶联DNA修复机制
  • 批准号:
    10669570
  • 财政年份:
    2022
  • 资助金额:
    $ 48.66万
  • 项目类别:
Chameleon Sample Preparation Device for Cryo-EM
用于冷冻电镜的变色龙样品制备装置
  • 批准号:
    10440804
  • 财政年份:
    2022
  • 资助金额:
    $ 48.66万
  • 项目类别:
Mechanism of cytoskeletal transport and transcription-coupled DNA repair
细胞骨架运输和转录偶联DNA修复机制
  • 批准号:
    10795265
  • 财政年份:
    2022
  • 资助金额:
    $ 48.66万
  • 项目类别:
Regulation of Cytoplasmic Dynein
细胞质动力蛋白的调节
  • 批准号:
    8867260
  • 财政年份:
    2014
  • 资助金额:
    $ 48.66万
  • 项目类别:
Regulation of Cytoplasmic Dynein
细胞质动力蛋白的调节
  • 批准号:
    9206422
  • 财政年份:
    2014
  • 资助金额:
    $ 48.66万
  • 项目类别:
Regulation of Cytoplasmic Dynein
细胞质动力蛋白的调节
  • 批准号:
    9278236
  • 财政年份:
    2014
  • 资助金额:
    $ 48.66万
  • 项目类别:
Regulation of Cytoplasmic Dynein
细胞质动力蛋白的调节
  • 批准号:
    10224220
  • 财政年份:
    2014
  • 资助金额:
    $ 48.66万
  • 项目类别:
A comparative structural study of ATP-dependent chromatin remodeling complexes
ATP依赖性染色质重塑复合物的比较结构研究
  • 批准号:
    8099202
  • 财政年份:
    2011
  • 资助金额:
    $ 48.66万
  • 项目类别:
A comparative structural study of ATP-dependent chromatin remodeling complexes
ATP依赖性染色质重塑复合物的比较结构研究
  • 批准号:
    10220986
  • 财政年份:
    2011
  • 资助金额:
    $ 48.66万
  • 项目类别:

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