GmGPA3 is involved in post-Golgi trafficking of storage proteins and cell growth in soybean cotyledons
文献类型: 外文期刊
第一作者: Wei, Zhongyan
作者: Wei, Zhongyan;Chen, Yu;Ren, Yulong;Qiu, Lijuan;Wei, Zhongyan;Zhang, Bo
作者机构:
关键词: Glycine max; Protein storage vacuole; Storage protein sorting; Transient RNAi
期刊名称:PLANT SCIENCE ( 影响因子:4.729; 五年影响因子:5.132 )
ISSN: 0168-9452
年卷期: 2020 年 294 卷
页码:
收录情况: SCI
摘要: As the major nutritional component in soybean seeds storage proteins are initially synthesized on the endoplasmic reticulum as precursors and subsequently delivered to protein storage vacuoles (PSVs) via the Golgimediated pathway where they are converted into mature subunits and accumulated. However, the molecular machinery required for storage protein trafficking in soybean remains largely unknown. In this study, we cloned the sole soybean homolog of OsGPA3 that encodes a plant-unique kelch-repeat regulator of post-Golgi vesicular traffic for rice storage protein sorting. A complementation test showed that GmGPA3 could rescue the rice gpa3 mutant. Biochemical assays verified that GmGPA3 physically interacts with GmRab5 and its guanine exchange factor (GEF) GmVPS9. Expression of GmGPA3 had no obvious effect on the GEF activity of GmVPS9 toward GmRab5a. Notably, knock-down of GmGPA3 disrupted the trafficking of mmRFP-CT10 (an artificial cargo destined for PSVs) in developing soybean cotyledons. We identified two putative GmGPA3 interacting partners (GmGMG3 and GmGMG11) by screening a yeast cDNA library. Overexpression of GmGPA3 or GmGMG3 caused shrunken cotyledon cells. Our overall results suggested that GmGPA3 plays an important role in cell growth and development, in addition to its conserved role in mediating storage protein trafficking in soybean cotyledons.
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