Phylogeny of the SNARE vesicle fusion machinery yields insights into the conservation of the secretory pathway in fungi.

Phylogeny of the SNARE vesicle fusion machinery yields insights into the conservation of the secretory pathway in fungi.
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DOI:
10.1186/1471-2148-9-19
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发表时间:
2009-01-23
影响因子:
3.4
通讯作者:
Fasshauer D
Fasshauer D
中科院分区:
生物学2区
文献类型:
--
作者:
Kienle N;Kloepper TH;Fasshauer D

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在真核细胞中,膜系统不同区室之间的定向运输是由囊泡介导的,囊泡从供体细胞器中萌发,然后与受体细胞器融合。一个完整的膜蛋白家族,被称为可溶性n -乙基马来酰亚胺敏感因子附着受体(SNARE)蛋白,构成了这些不同膜融合事件的关键机制。在过去的30年里,酿酒酵母一直是研究其分泌和内吞途径组织的一个强大的模式生物,几年前,它的一整套SNAREs被编制完成。在这里,我们利用越来越多的基因组数据来研究SNARE家族在真菌进化过程中的历史。此外,由于不同的SNARE家族成员被认为划分不同的细胞器和囊泡,这种方法使我们能够比较酵母和动物细胞的膜系统的组织。我们的数据证实了真菌通常包含一组相对简单的SNARE蛋白的观点,这些SNARE蛋白主要包括原真核细胞的SNARE。然而,所有真菌都含有一种新的可溶性SNARE蛋白Vam7,它携带一个n端px结构域,作为磷酸肌苷结合模块。此外,可以确定真菌进化中发生谱系特异性复制和多样化的点。例如,内体合成酶Pep12和Vam3产生于Saccharomycotina分支中的基因复制。尽管面包师酵母的SNARE曲目高度保守,但我们的分析表明,它比基础真菌的曲目更偏离。这突出表明,面包酵母的运输途径不仅与动物细胞不同,而且与许多其他真菌的运输途径也有所不同。
In eukaryotic cells, directional transport between different compartments of the endomembrane system is mediated by vesicles that bud from a donor organelle and then fuse with an acceptor organelle. A family of integral membrane proteins, termed soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins, constitute the key machineries of these different membrane fusion events. Over the past 30 years, the yeast Saccharomyces cerevisiae has served as a powerful model organism for studying the organization of the secretory and endocytic pathways, and a few years ago, its entire set of SNAREs was compiled. Here, we make use of the increasing amount of genomic data to investigate the history of the SNARE family during fungi evolution. Moreover, since different SNARE family members are thought to demarcate different organelles and vesicles, this approach allowed us to compare the organization of the endomembrane systems of yeast and animal cells. Our data corroborate the notion that fungi generally encompass a relatively simple set of SNARE proteins, mostly comprising the SNAREs of the proto-eukaryotic cell. However, all fungi contain a novel soluble SNARE protein, Vam7, which carries an N-terminal PX-domain that acts as a phosphoinositide binding module. In addition, the points in fungal evolution, at which lineage-specific duplications and diversifications occurred, could be determined. For instance, the endosomal syntaxins Pep12 and Vam3 arose from a gene duplication that occurred within the Saccharomycotina clade. Although the SNARE repertoire of baker's yeast is highly conserved, our analysis reveals that it is more deviated than the ones of basal fungi. This highlights that the trafficking pathways of baker's yeast are not only different to those in animal cells but also are somewhat different to those of many other fungi.
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