Myosin V attachment to cargo requires the tight association of two functional subdomains.

Myosin V attachment to cargo requires the tight association of two functional subdomains.
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肌球蛋白V附着货物需要两个功能子域的紧密关联。

DOI:
10.1083/jcb.200407146
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发表时间:
2005-01-31
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Weisman LS
Weisman LS
中科院分区:
其他
文献类型:
--
作者:
Pashkova N;Catlett NL;Novak JL;Wu G;Lu R;Cohen RE;Weisman LS

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肌球蛋白 V 羧基末端球状尾结构域对于肌球蛋白 V 与所有已知货物的附着至关重要。此前,球状尾巴被视为一个单一的功能实体。在这里,我们发现酵母肌球蛋白 Va 同源物 Myo2p 的球状尾包含两个具有不同功能的结构子结构域,即液泡特异性和分泌囊泡特异性运动。生化和遗传分析表明,子结构域 I 与子结构域 II 紧密相关,并且这种相互作用不需要额外的蛋白质。重要的是,虽然两个子结构域单独都没有功能,但单独的子结构域的同时表达在体内产生功能复合物。我们的结果提出了一个模型,通过该模型,球状尾部子域之间的分子内相互作用有助于协调肌球蛋白 V 多种不同货物的运输。
The myosin V carboxyl-terminal globular tail domain is essential for the attachment of myosin V to all known cargoes. Previously, the globular tail was viewed as a single, functional entity. Here, we show that the globular tail of the yeast myosin Va homologue, Myo2p, contains two structural subdomains that have distinct functions, namely, vacuole-specific and secretory vesicle–specific movement. Biochemical and genetic analyses demonstrate that subdomain I tightly associates with subdomain II, and that the interaction does not require additional proteins. Importantly, although neither subdomain alone is functional, simultaneous expression of the separate subdomains produces a functional complex in vivo. Our results suggest a model whereby intramolecular interactions between the globular tail subdomains help to coordinate the transport of multiple distinct cargoes by myosin V.
DOI: 10.1083/jcb.153.1.47
发表时间: 2001-04-02
期刊: The Journal of cell biology
影响因子: --
作者:
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