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Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain
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Nezis, I. P., Simonsen, Anne, Sagona, Antonia P., Finley, Kim D., Gaumer, S., Contamine, D., Rusten, Tor Erik, Stenmark, H. (Harald) and Brech, Andreas (2008) Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain. The Journal of Cell Biology, Vol. 180 (No. 6). pp. 1065-1071. doi:10.1083/jcb.200711108 ISSN 0021-9525.
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Official URL: http://dx.doi.org/10.1083/jcb.200711108
Abstract
p62 has been proposed to mark ubiquitinated protein bodies for autophagic degradation. We report that the Drosophila melanogaster p62 orthologue, Ref(2)P, is a regulator of protein aggregation in the adult brain. We demonstrate that Ref(2)P localizes to age-induced protein aggregates as well as to aggregates caused by reduced autophagic or proteasomal activity. A similar localization to protein aggregates is also observed in D. melanogaster models of human neurodegenerative diseases. Although atg8a autophagy mutant flies show accumulation of ubiquitin- and Ref(2)P-positive protein aggregates, this is abrogated in atg8a/ref(2)P double mutants. Both the multimerization and ubiquitin binding domains of Ref(2)P are required for aggregate formation in vivo. Our findings reveal a major role for Ref(2)P in the formation of ubiquitin-positive protein aggregates both under physiological conditions and when normal protein turnover is inhibited.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | The Journal of Cell Biology | ||||
Publisher: | The Rockefeller University Press | ||||
ISSN: | 0021-9525 | ||||
Official Date: | 2008 | ||||
Dates: |
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Volume: | Vol. 180 | ||||
Number: | No. 6 | ||||
Page Range: | pp. 1065-1071 | ||||
DOI: | 10.1083/jcb.200711108 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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