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<p>Endoplasmic reticulum exit sites (ERESs) are ER subdomains where coat protein complex II carriers are assembled for ER-to-Golgi transport. We previously proposed a dynamic capture-and-release model of ERESs by Golgi stacks in plants. However, how ERESs and Golgi stacks maintain a stable interaction in plant cells with vigorous cytoplasmic streaming is unknown. Here, we show that a plant-specific ER transmembrane protein, which we designate as MAG3, plays a crucial role in mediating the capture-and-release of ERESs in Arabidopsis. We isolated a mutant (<i>mag3</i>) defective in protein exit from the ER in seeds. MAG3 localized specifically to the ER-Golgi interface with Golgi-associated ERESs and remained there after ERES release. MAG3 deficiency caused a reduction in the amount of ERESs associated with each Golgi stack. MAG3 interacted with WPP DOMAIN PROTEINs, which are also plant-specific. These results suggest that plants have evolved a unique system to support ER-to-Golgi transport despite intracellular motility.</p>

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Plant-specific tail-anchored coiled-coil protein MAG3 stabilizes Golgi-associated ERESs to facilitate protein exit from the ER

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年3月4日

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  • Junpei Takagi,
  • Hideyuki Takahashi,
  • Kenta C. Moriya,
  • Minoru Nagano,
  • Yoichiro Fukao,
  • Haruko Ueda,
  • Kentaro Tamura,
  • Tomoo Shimada,
  • Ikuko Hara-Nishimura

摘要

Endoplasmic reticulum exit sites (ERESs) are ER subdomains where coat protein complex II carriers are assembled for ER-to-Golgi transport. We previously proposed a dynamic capture-and-release model of ERESs by Golgi stacks in plants. However, how ERESs and Golgi stacks maintain a stable interaction in plant cells with vigorous cytoplasmic streaming is unknown. Here, we show that a plant-specific ER transmembrane protein, which we designate as MAG3, plays a crucial role in mediating the capture-and-release of ERESs in Arabidopsis. We isolated a mutant (mag3) defective in protein exit from the ER in seeds. MAG3 localized specifically to the ER-Golgi interface with Golgi-associated ERESs and remained there after ERES release. MAG3 deficiency caused a reduction in the amount of ERESs associated with each Golgi stack. MAG3 interacted with WPP DOMAIN PROTEINs, which are also plant-specific. These results suggest that plants have evolved a unique system to support ER-to-Golgi transport despite intracellular motility.