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

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Τίτλος: Reversible control of post-Golgi transport by brefeldin A reveals recycling endosome maturation during glycosylphosphatidylinositol-anchored protein transport.
Συγγραφείς: Takiguchi A; Graduate School of Integrated Sciences for Life, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, Japan., Shek HT; Graduate School of Integrated Sciences for Life, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, Japan., Sasaki S; Graduate School of Integrated Sciences for Life, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, Japan., Tago T; Graduate School of Integrated Sciences for Life, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, Japan., Uehara T; Graduate School of Integrated Sciences for Life, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, Japan., Goto Y; Technology Platform Division, Mass Spectrometry and Microscopy Unit, RIKEN Center for Sustainable Resource Science, Yokohama, Kanagawa, Japan., Toyooka K; Technology Platform Division, Mass Spectrometry and Microscopy Unit, RIKEN Center for Sustainable Resource Science, Yokohama, Kanagawa, Japan., Kurokawa K; Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, 2-1 Hirosawa, Wako, Saitama, Japan., Tojima T; Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, 2-1 Hirosawa, Wako, Saitama, Japan.; Image Processing Research Team, RIKEN Center for Advanced Photonics, Wako, Saitama, Japan., Nakano A; Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, 2-1 Hirosawa, Wako, Saitama, Japan.; Image Processing Research Team, RIKEN Center for Advanced Photonics, Wako, Saitama, Japan.; Institute of Integrated Research, Science Tokyo, Chiyoda-ku, Tokyo, Japan., Maeda M; Core Facility Management Center, Hiroshima University, Higashi-Hiroshima, Hiroshima, Japan., Satoh T; Graduate School of Integrated Sciences for Life, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, Japan. tsatoh3@hiroshima-u.ac.jp.; Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, 2-1 Hirosawa, Wako, Saitama, Japan. tsatoh3@hiroshima-u.ac.jp., Satoh AK; Graduate School of Integrated Sciences for Life, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, Japan. aksatoh@hiroshima-u.ac.jp.; Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, 2-1 Hirosawa, Wako, Saitama, Japan. aksatoh@hiroshima-u.ac.jp.
Πηγή: Nature communications [Nat Commun] 2026 Jul 27; Vol. 17 (1). Date of Electronic Publication: 2026 Jul 27.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
Imprint Name(s): Original Publication: [London] : Nature Pub. Group
Ιατρικοί όροι (MeSH): Brefeldin A*/pharmacology , Glycosylphosphatidylinositols*/metabolism , Endosomes*/metabolism , Endosomes*/drug effects , Endosomes*/ultrastructure , Golgi Apparatus*/metabolism , Golgi Apparatus*/drug effects, Protein Transport/drug effects ; trans-Golgi Network/metabolism ; trans-Golgi Network/drug effects ; trans-Golgi Network/ultrastructure ; Cell Membrane/metabolism ; Humans ; Animals ; HeLa Cells
Περίληψη: 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.
(© 2026. The Author(s).)
Competing Interests: Competing interests: The authors declare no competing interests.
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Grant Information: JPMJCR22E2 MEXT | JST | Core Research for Evolutional Science and Technology (CREST)
Molecular Sequence: figshare doi.org/10.6084/m9.figshare.32684082
Substance Nomenclature: 20350-15-6 (Brefeldin A)
0 (Glycosylphosphatidylinositols)
Entry Date(s): Date Created: 20260727 Date Completed: 20260729 Latest Revision: 20260813
Update Code: 20260814
PubMed Central ID: PMC13408501
DOI: 10.1038/s41467-026-75784-1
PMID: 42509243
Βάση Δεδομένων: MEDLINE
Περιγραφή
ISSN:2041-1723
DOI:10.1038/s41467-026-75784-1