p47 is a cofactor for p97-mediated membrane fusion (2024)

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Abstract Access options Additional access options: Similar content being viewed by others The many functions of ESCRTs Mechanisms of SNARE proteins in membrane fusion Structure of a membrane tethering complex incorporating multiple SNAREs References Acknowledgements Author information Authors and Affiliations Corresponding author Rights and permissions About this article Cite this article This article is cited by In silico prediction, characterization, docking studies and molecular dynamics simulation of human p97 in complex with p37 cofactor The determination of the relationship between p97/VCP, small VCP-interacting protein, two ERAD proteins and steroidogenesis in Leydig cell lines Degradation of p47 by autophagy contributes to CADM1 overexpression in ATLL cells through the activation of NF-κB The involvement of endoplasmic reticulum formation and protein synthesis efficiency in VCP- and ATL1-related neurological disorders UBXN3B positively regulates STING-mediated antiviral immune responses Comments
  • Letter
  • Published:
  • Hisao Kondo1,
  • Catherine Rabouille1,
  • Richard Newman2,
  • Timothy P. Levine4,
  • Darryl Pappin3,
  • Paul Freemont2 &
  • …
  • Graham Warren1

Nature volume388,pages 75–78 (1997)Cite this article

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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 hom*otypic 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 hom*ologue 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.

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Similar content being viewed by others

p47 is a cofactor for p97-mediated membrane fusion (6)

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p47 is a cofactor for p97-mediated membrane fusion (7)

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p47 is a cofactor for p97-mediated membrane fusion (8)

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Acknowledgements

We thank T. Chappell, F. Barr, B. Svejstrup, B. Sönnichsen, M. Lowe, C. Fernandez, D. Shima, J. Shorter, N. Hui and A. Coffer for helpful comments and for reagents; G. Banting for the rat liver cDNA library; J.-M. Peters for monoclonal anti-p97 antibodies; G. Clark and A. Davies for DNA sequencing; and D. Rahman for protein sequencing. Special thanks go to N. Nakamura for advice.

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Authors and Affiliations

  1. *Cell Biology Laboratory Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London, WC2A 3PX, UK

    Hisao Kondo,Catherine Rabouille&Graham Warren

  2. †Protein Structure Laboratory Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London, WC2A 3PX, UK

    Richard Newman&Paul Freemont

  3. §Protein Sequencing Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London, WC2A 3PX, UK

    Darryl Pappin

  4. ‡MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Timothy P. Levine

Authors

  1. Hisao Kondo

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  2. Catherine Rabouille

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  3. Richard Newman

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  4. Timothy P. Levine

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  5. Darryl Pappin

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  6. Paul Freemont

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  7. Graham Warren

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Correspondence to Graham Warren.

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Kondo, H., Rabouille, C., Newman, R. et al. p47 is a cofactor for p97-mediated membrane fusion. Nature 388, 75–78 (1997). https://doi.org/10.1038/40411

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p47 is a cofactor for p97-mediated membrane fusion (2024)
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