p47 is a cofactor for p97-mediated membrane fusion View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1997-07

AUTHORS

Hisao Kondo, Catherine Rabouille, Richard Newman, Timothy P. Levine, Darryl Pappin, Paul Freemont, Graham Warren

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. More... »

PAGES

75-78

References to SciGraph publications

Journal

TITLE

Nature

ISSUE

6637

VOLUME

388

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/40411

    DOI

    http://dx.doi.org/10.1038/40411

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1010703254

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9214505


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