A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways

Meyer, H. H., Shorter, J. G., Seemann, J., Pappin, D., Warren, G. (May 2000) A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J, 19 (10). pp. 2181-92. ISSN 0261-4189 (Print)0261-4189 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/10811609
DOI: 10.1093/emboj/19.10.2181

Abstract

The AAA-ATPase, p97/Cdc48p, has been implicated in many different pathways ranging from membrane fusion to ubiquitin-dependent protein degradation. Binding of the p47 complex directs p97 to act in the post-mitotic fusion of Golgi membranes. We now describe another binding complex comprising mammalian Ufd1 and Npl4. Yeast Ufd1p is required for ubiquitin-dependent protein degradation whereas yeast Npl4p has been implicated in nuclear transport. In rat liver cytosol, Ufd1 and Npl4 form a binary complex, which exists either alone or bound to p97. Ufd1/Npl4 competes with p47 for binding to p97 and so inhibits Golgi membrane fusion. This suggests that it is involved in another cellular function catalysed by p97, the most likely being ubiquitin-dependent events during mitosis. The fact that the binding of p47 and Ufd1/Npl4 is mutually exclusive suggests that these protein complexes act as adapters, directing a basic p97 activity into different cellular pathways.

Item Type: Paper
Uncontrolled Keywords: Adenosine Triphosphatases/ metabolism Amino Acid Sequence Animals Base Sequence Biological Transport Cell Cycle Proteins/ metabolism Cell Nucleus/ metabolism Liver/metabolism Mice Molecular Sequence Data Nuclear Pore Complex Proteins Nuclear Proteins/metabolism Nucleocytoplasmic Transport Proteins Proteins/ metabolism Rats Saccharomyces cerevisiae Proteins Ubiquitins/ metabolism
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein ubiquitination
CSHL Authors:
Communities: CSHL labs > Pappin lab
Depositing User: Matt Covey
Date: 15 May 2000
Date Deposited: 31 Jan 2014 20:10
Last Modified: 31 Jan 2014 20:10
PMCID: PMC384367
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29367

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