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Sequential interactions with Sec23 control the direction of vesicle traffic

Author

Listed:
  • Christopher Lord

    (Howard Hughes Medical Institute, University of California at San Diego)

  • Deepali Bhandari

    (Howard Hughes Medical Institute, University of California at San Diego)

  • Shekar Menon

    (Howard Hughes Medical Institute, University of California at San Diego)

  • Majid Ghassemian

    (Biomolecular and Proteomics Mass Spectrometry Facility, University of California at San Diego)

  • Deborah Nycz

    (The University of Montana)

  • Jesse Hay

    (The University of Montana)

  • Pradipta Ghosh

    (University of California at San Diego)

  • Susan Ferro-Novick

    (Howard Hughes Medical Institute, University of California at San Diego)

Abstract

How the directionality of vesicle traffic is achieved remains an important unanswered question in cell biology. The Sec23p/Sec24p coat complex sorts the fusion machinery (SNAREs) into vesicles as they bud from the endoplasmic reticulum (ER). Vesicle tethering to the Golgi begins when the tethering factor TRAPPI binds to Sec23p. Where the coat is released and how this event relates to membrane fusion is unknown. Here we use a yeast transport assay to demonstrate that an ER-derived vesicle retains its coat until it reaches the Golgi. A Golgi-associated kinase, Hrr25p (CK1δ orthologue), then phosphorylates the Sec23p/Sec24p complex. Coat phosphorylation and dephosphorylation are needed for vesicle fusion and budding, respectively. Additionally, we show that Sec23p interacts in a sequential manner with different binding partners, including TRAPPI and Hrr25p, to ensure the directionality of ER–Golgi traffic and prevent the back-fusion of a COPII vesicle with the ER. These events are conserved in mammalian cells.

Suggested Citation

  • Christopher Lord & Deepali Bhandari & Shekar Menon & Majid Ghassemian & Deborah Nycz & Jesse Hay & Pradipta Ghosh & Susan Ferro-Novick, 2011. "Sequential interactions with Sec23 control the direction of vesicle traffic," Nature, Nature, vol. 473(7346), pages 181-186, May.
    • Handle: RePEc:nat:nature:v:473:y:2011:i:7346:d:10.1038_nature09969
    DOI: 10.1038/nature09969
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    Cited by:

    1. Rita Rosado-Ramos & Gonçalo M. Poças & Daniela Marques & Alexandre Foito & David M. Sevillano & Mafalda Lopes-da-Silva & Luís G. Gonçalves & Regina Menezes & Marcel Ottens & Derek Stewart & Alain Ibáñ, 2023. "Genipin prevents alpha-synuclein aggregation and toxicity by affecting endocytosis, metabolism and lipid storage," Nature Communications, Nature, vol. 14(1), pages 1-21, December.

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