The Sar1 GTPase coordinates biosynthetic cargo selection with endoplasmic reticulum export site assembly.

The Sar1 GTPase coordinates biosynthetic cargo selection with endoplasmic reticulum export site assembly.
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DOI:
10.1083/jcb.152.1.213
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发表时间:
2001-01-08
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Balch WE
Balch WE
中科院分区:
其他
文献类型:
--
作者:
Aridor M;Fish KN;Bannykh S;Weissman J;Roberts TH;Lippincott-Schwartz J;Balch WE

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内质网的货物选择和输出是由COPII包衣机制介导的,其中包括小的GTPase Sar1和Sec23/24和Sec13/31复合体。我们分析了纯化的Sar1和COPII包衣复合体在体外从ER同步出口货物过程中调节的一系列事件。我们发现,在没有其他胞液成分的情况下,仅激活Sar1就会导致内质网衍生的管状结构域的形成,这些结构域类似于启动货物选择的内质网过渡元件。这些由Sar1产生的管状结构域在体外被证明是内质网到高尔基体转运的瞬时的、功能性的中间体。通过跟踪活细胞中的货物输出,我们发现体内的内质网输出也以动态管状结构的形成为特征。我们的结果表明,Sar1在通过产生过渡性管状ER出口位点将货物选择与ER形态发生联系起来方面发挥了意想不到的新作用。
Cargo selection and export from the endoplasmic reticulum is mediated by the COPII coat machinery that includes the small GTPase Sar1 and the Sec23/24 and Sec13/31 complexes. We have analyzed the sequential events regulated by purified Sar1 and COPII coat complexes during synchronized export of cargo from the ER in vitro. We find that activation of Sar1 alone, in the absence of other cytosolic components, leads to the formation of ER-derived tubular domains that resemble ER transitional elements that initiate cargo selection. These Sar1-generated tubular domains were shown to be transient, functional intermediates in ER to Golgi transport in vitro. By following cargo export in live cells, we show that ER export in vivo is also characterized by the formation of dynamic tubular structures. Our results demonstrate an unanticipated and novel role for Sar1 in linking cargo selection with ER morphogenesis through the generation of transitional tubular ER export sites.
DOI: 10.1016/0092-8674(94)90359-x
发表时间: 1994-03-11
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影响因子: 64.5
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