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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Bagley, Joshua A. Rumpf, Sebastian Thompson-peer, Katherine L. Beckstead, Robert B. Zhu, Sijun Gorczyca, David Jan, Lily Yeh Jan, Yuh Nung |
| Description | Author Affiliation: Rumpf S ( Howard Hughes Medical Institute andDepartments of Physiology andBiochemistry, University of California, San Francisco, CA 94158); Bagley JA ( Howard Hughes Medical Institute andDepartments of Physiology andBiochemistry, University of California, San Francisco, CA 94158); Thompson-Peer KL ( Howard Hughes Medical Institute andDepartments of Physiology andBiochemistry, University of California, San Francisco, CA 94158); Zhu S ( Howard Hughes Medical Institute andDepartments of Physiology andBiochemistry, University of California, San Francisco, CA 94158); Gorczyca D ( Howard Hughes Medical Institute andDepartments of Physiology andBiochemistry, University of California, San Francisco, CA 94158); Beckstead RB ( Poultry Science Department, University of Georgia, Athens, GA 30602.); Jan LY ( Howard Hughes Medical Institute andDepartments of Physiology andBiochemistry, University of California, San Francisco, CA 94158); Jan YN ( Howard Hughes Medical Institute andDepartments of Physiology andBiochemistry, University of California, San Francisco, CA 94158); |
| Abstract | The dendritic arbors of the larval Drosophila peripheral class IV dendritic arborization neurons degenerate during metamorphosis in an ecdysone-dependent manner. This process-also known as dendrite pruning-depends on the ubiquitin-proteasome system (UPS), but the specific processes regulated by the UPS during pruning have been largely elusive. Here, we show that mutation or inhibition of Valosin-Containing Protein (VCP), a ubiquitin-dependent ATPase whose human homolog is linked to neurodegenerative disease, leads to specific defects in mRNA metabolism and that this role of VCP is linked to dendrite pruning. Specifically, we find that VCP inhibition causes an altered splicing pattern of the large pruning gene molecule interacting with CasL and mislocalization of the Drosophila homolog of the human RNA-binding protein TAR-DNA-binding protein of 43 kilo-Dalton (TDP-43). Our data suggest that VCP inactivation might lead to specific gain-of-function of TDP-43 and other RNA-binding proteins. A similar combination of defects is also seen in a mutant in the ubiquitin-conjugating enzyme ubcD1 and a mutant in the 19S regulatory particle of the proteasome, but not in a 20S proteasome mutant. Thus, our results highlight a proteolysis-independent function of the UPS during class IV dendritic arborization neuron dendrite pruning and link the UPS to the control of mRNA metabolism. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 20 |
| Volume Number | 111 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2014-05-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Triphosphatases Physiology Dendrites Metabolism Drosophila Proteins Gene Expression Regulation RNA, Messenger Animals DNA-Binding Proteins Drosophila Melanogaster Ecdysone Mutation Neurons Phenotype Proteasome Endopeptidase Complex Protein Binding RNA-Binding Proteins Signal Transduction Ubiquitin Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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