The canonical α-SNAP is essential for gametophytic development in Arabidopsis.
The canonical α-SNAP is essential for gametophytic development in Arabidopsis.
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典型的 α-SNAP 对于拟南芥配子体发育至关重要
DOI：
10.1371/journal.pgen.1009505
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发表时间：
2021-04
期刊：
影响因子：
4.5
通讯作者：
Zhang Y
中科院分区：
文献类型：
--
作者：
Liu F;Li JP;Li LS;Liu Q;Li SW;Song ML;Li S;Zhang Y
雌雄配子体的发育是被子植物成功繁殖的先决条件。介导囊泡运输的因子是控制配子体发育的关键调节因子之一。囊泡和靶膜之间的融合需要融合可溶性N-乙基马来酰亚胺敏感因子附着蛋白受体（SNARE）复合物的组装，其分解反过来确保单个SNARE组分的再循环。融合后SNARE复合物的分解由酵母和后生动物中的AAA+ ATP酶N-乙基马来酰亚胺敏感因子（Sec 18/NSF）和可溶性NSF附着蛋白（Sec 17/α-SNAP）控制。尽管非典型α-SNAP在大豆中已被功能性地表征，但典型α-SNAP的生物学功能尚未在植物中被证实。我们在这里报告，典型的α-SNAP在拟南芥中是必不可少的男性和女性配子体发育。拟南芥中典型α-SNAP的功能缺失通过阻止配子发生过程中的第一次有丝分裂而导致配子体致死。我们进一步表明，拟南芥α-SNAP编码两个异构体由于选择性剪接。这两种异构体相互作用与拟南芥同源的NSF，而有不同的亚细胞定位。人α-SNAP的相似选择性剪接的存在表明两种α-SNAP异构体的功能差异在进化上是保守的。
The development of male and female gametophytes is a pre-requisite for successful reproduction of angiosperms. Factors mediating vesicular trafficking are among the key regulators controlling gametophytic development. Fusion between vesicles and target membranes requires the assembly of a fusogenic soluble N-ethylmaleimide sensitive factor attachment protein receptors (SNAREs) complex, whose disassembly in turn ensures the recycle of individual SNARE components. The disassembly of post-fusion SNARE complexes is controlled by the AAA+ ATPase N-ethylmaleimide-sensitive factor (Sec18/NSF) and soluble NSF attachment protein (Sec17/α-SNAP) in yeast and metazoans. Although non-canonical α-SNAPs have been functionally characterized in soybeans, the biological function of canonical α-SNAPs has yet to be demonstrated in plants. We report here that the canonical α-SNAP in Arabidopsis is essential for male and female gametophytic development. Functional loss of the canonical α-SNAP in Arabidopsis results in gametophytic lethality by arresting the first mitosis during gametogenesis. We further show that Arabidopsis α-SNAP encodes two isoforms due to alternative splicing. Both isoforms interact with the Arabidopsis homolog of NSF whereas have distinct subcellular localizations. The presence of similar alternative splicing of human α-SNAP indicates that functional distinction of two α-SNAP isoforms is evolutionarily conserved.
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