Grain setting defect1 (GSD1) function in rice depends on S-acylation and interacts with actin 1 (OsACT1) at its C-terminal.
Grain setting defect1 (GSD1) function in rice depends on S-acylation and interacts with actin 1 (OsACT1) at its C-terminal.
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DOI：
10.3389/fpls.2015.00804
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发表时间：
2015
影响因子：
5.6
通讯作者：
Li L
中科院分区：
文献类型：
--
作者：
Gui J;Zheng S;Shen J;Li L
结实缺陷蛋白1（GSD 1）是一种植物特异性表达的蛋白质，定位于韧皮部伴胞的质膜和胞间连丝上，通过调节光合产物的运输来影响水稻结实。在这里，我们展示了新的证据表明，GSD 1是本地化的PM和一段45个氨基酸残基在其C-末端的细胞质面是必需的，其本地化。与PM的关联是由半胱氨酸残基Cys-524和Cys-527的S-酰化介导的，在水稻中GSD 1功能所必需的45个氨基酸残基的序列中。此外，GSD 1中的卷曲螺旋结构域对于与OsACT 1的充分相互作用是必要的。总之，这些结果表明，GSD 1通过S-酰化连接到PM和OsACT 1通过其卷曲螺旋结构域相互作用，以调节水稻光合同化物运输的胞间连丝电导。
Grain setting defect1 (GSD1), a plant-specific remorin protein specifically localized at the plasma membrane (PM) and plasmodesmata of phloem companion cells, affects grain setting in rice through regulating the transport of photoassimilates. Here, we show new evidence demonstrating that GSD1 is localized at the cytoplasmic face of the PM and a stretch of 45 amino acid residues at its C-terminal is required for its localization. Association with the PM is mediated by S-acylation of cysteine residues Cys-524 and Cys-527, in a sequence of 45 amino acid residues essential for GSD1 function in rice. Furthermore, the coiled-coil domain in GSD1 is necessary for sufficient interaction with OsACT1. Together, these results reveal that GSD1 attaches to the PM through S-acylation and interacts with OsACT1 through its coiled-coil domain structure to regulate plasmodesmata conductance for photoassimilate transport in rice.