The dynamin-like GTPase Sey1p mediates homotypic ER fusion in S. cerevisiae.

The dynamin-like GTPase Sey1p mediates homotypic ER fusion in S. cerevisiae.
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DOI:
10.1083/jcb.201111115
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发表时间:
2012-04-16
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Prinz WA
Prinz WA
中科院分区:
其他
文献类型:
--
作者:
Anwar K;Klemm RW;Condon A;Severin KN;Zhang M;Ghirlando R;Hu J;Rapoport TA;Prinz WA

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芽殖酵母Sey 1 p的功能类似于哺乳动物atlastins介导的ER融合,通过一种机制,这是多余的第二,ER陷阱介导的融合机制。内质网(ER)形成一个需要同型膜融合来维持的小管和片的网络。在后生动物中,这一过程由称为atlastins(ATL)的动力蛋白样鸟苷三磷酸酶(GTP酶)介导,这也是维持ER形态所必需的。先前的工作表明,需要动力蛋白样GTdR Sey 1 p来维持酿酒酵母中的ER形态。在本文中,我们证明,Sey 1 p,像ATLs,介导同型ER融合。Sey 1 p的缺乏导致ER在体内进行延迟融合,并且含有纯化Sey 1 p的蛋白脂质体在体外以GTP依赖的方式融合。Sey 1 p在体内可被ATL 1部分取代。与ATL 1一样,Sey 1 p也经历了GTP依赖的二聚化。我们发现缺乏Sey 1 p的细胞中发生的残留ER-ER融合需要ER陷阱Ufe 1 p。总的来说,我们的研究结果表明,Sey 1 p和它的同系物功能类似于ATLs介导ER融合。它们还表明S.酿酒酵母具有需要ER SNARE的替代融合机制。
Budding yeast Sey1p functions analogously to mammalian atlastins in mediating ER fusion through a mechanism that is redundant with a second, ER SNARE-mediated fusion mechanism. The endoplasmic reticulum (ER) forms a network of tubules and sheets that requires homotypic membrane fusion to be maintained. In metazoans, this process is mediated by dynamin-like guanosine triphosphatases (GTPases) called atlastins (ATLs), which are also required to maintain ER morphology. Previous work suggested that the dynamin-like GTPase Sey1p was needed to maintain ER morphology in Saccharomyces cerevisiae. In this paper, we demonstrate that Sey1p, like ATLs, mediates homotypic ER fusion. The absence of Sey1p resulted in the ER undergoing delayed fusion in vivo and proteoliposomes containing purified Sey1p fused in a GTP-dependent manner in vitro. Sey1p could be partially replaced by ATL1 in vivo. Like ATL1, Sey1p underwent GTP-dependent dimerization. We found that the residual ER–ER fusion that occurred in cells lacking Sey1p required the ER SNARE Ufe1p. Collectively, our results show that Sey1p and its homologues function analogously to ATLs in mediating ER fusion. They also indicate that S. cerevisiae has an alternative fusion mechanism that requires ER SNAREs.
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