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<p>Post-Golgi transport plays a crucial role in establishing and maintaining cellular function; however, its mechanism of action remains unclear. Therefore, a system to manipulate post-Golgi transport is highly desirable. In this study, we developed a brefeldin A (BFA)-controlled system to block and restart post-Golgi transport freely, allowing the detailed observation of cargo exit from Golgi stacks using live-cell imaging, electron microscopy, and biochemical analysis. Using this system, glycosylphosphatidylinositol-anchored protein (GPI-AP) transport from the <i>trans</i>-Golgi network (TGN) to Golgi-associated recycling endosomes (GA-REs) was visualized. GA-REs expanded during GPI-AP uptake, indicating maturation from the TGN into REs, which later detached as free REs released from the Golgi stacks. Tubular and pearled GPI-AP-positive structures formed on the TGN, which were likely GA-REs transporting GPI-AP from the TGN. REs matured in AP-1-deficient cells, whereas GA-RE detachment was impaired, and long-tubules were observed, thereby delaying GPI-AP delivery to the plasma membrane.</p>

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Reversible control of post-Golgi transport by brefeldin A reveals recycling endosome maturation during glycosylphosphatidylinositol-anchored protein transport

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年7月27日

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  • Arata Takiguchi,
  • Ho Tung Shek,
  • Shogo Sasaki,
  • Tatsuya Tago,
  • Taisei Uehara,
  • Yumi Goto,
  • Kiminori Toyooka,
  • Kazuo Kurokawa,
  • Takuro Tojima,
  • Akihiko Nakano,
  • Makoto Maeda,
  • Takunori Satoh,
  • Akiko K. Satoh

摘要

Post-Golgi transport plays a crucial role in establishing and maintaining cellular function; however, its mechanism of action remains unclear. Therefore, a system to manipulate post-Golgi transport is highly desirable. In this study, we developed a brefeldin A (BFA)-controlled system to block and restart post-Golgi transport freely, allowing the detailed observation of cargo exit from Golgi stacks using live-cell imaging, electron microscopy, and biochemical analysis. Using this system, glycosylphosphatidylinositol-anchored protein (GPI-AP) transport from the trans-Golgi network (TGN) to Golgi-associated recycling endosomes (GA-REs) was visualized. GA-REs expanded during GPI-AP uptake, indicating maturation from the TGN into REs, which later detached as free REs released from the Golgi stacks. Tubular and pearled GPI-AP-positive structures formed on the TGN, which were likely GA-REs transporting GPI-AP from the TGN. REs matured in AP-1-deficient cells, whereas GA-RE detachment was impaired, and long-tubules were observed, thereby delaying GPI-AP delivery to the plasma membrane.