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p47 is a cofactor for p97-mediated membrane fusion

Author

Listed:
  • Hisao Kondo

    (*Cell Biology Laboratory Imperial Cancer Research Fund)

  • Catherine Rabouille

    (*Cell Biology Laboratory Imperial Cancer Research Fund)

  • Richard Newman

    (†Protein Structure Laboratory Imperial Cancer Research Fund)

  • Timothy P. Levine

    (‡MRC Laboratory of Molecular Biology)

  • Darryl Pappin

    (§Protein Sequencing Laboratory, Imperial Cancer Research Fund)

  • Paul Freemont

    (†Protein Structure Laboratory Imperial Cancer Research Fund)

  • Graham Warren

    (*Cell Biology Laboratory Imperial Cancer Research Fund)

Abstract

At least two distinct ATPases, NSF and p97, are known to be involved in the heterotypic fusion of transport vesicles with their target membranes and the homotypic fusion of membrane compartments1. The NSF-mediated fusion pathway is the best characterized, many of the components having been identified and their functions analysed2,3,4,5,6,7. In contrast, none of the accessory proteins for the p97-mediated fusion pathway has been identified8,9,10. Now we have identified the first such component, a protein of relative molecular mass 47,000 (p47), which forms a tight, stoichiometric complex with cytosolic p97 (one trimer of p47 per hexamer of p97). It is essential for the p97-mediated regrowth of Golgi cisternae from mitotic Golgi fragments, a process restricted to animal cells11. As a homologue of p47 exists in budding yeast, this indicates that it might also be involved in other membrane fusion reactions catalysed by p97, such as karyogamy10.

Suggested Citation

  • Hisao Kondo & Catherine Rabouille & Richard Newman & Timothy P. Levine & Darryl Pappin & Paul Freemont & Graham Warren, 1997. "p47 is a cofactor for p97-mediated membrane fusion," Nature, Nature, vol. 388(6637), pages 75-78, July.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6637:d:10.1038_40411
    DOI: 10.1038/40411
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    Cited by:

    1. Ian Cooney & Heidi L. Schubert & Karina Cedeno & Olivia N. Fisher & Richard Carson & John C. Price & Christopher P. Hill & Peter S. Shen, 2024. "Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Yang Xu & Han Han & Ian Cooney & Yuxuan Guo & Noah G. Moran & Nathan R. Zuniga & John C. Price & Christopher P. Hill & Peter S. Shen, 2022. "Active conformation of the p97-p47 unfoldase complex," Nature Communications, Nature, vol. 13(1), pages 1-8, December.

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