The Ubiquitin Receptor S5a/Rpn10 Links Centrosomal Proteasomes with Dendrite Development in the Mammalian Brain
Proteasomes drive the selective degradation of protein substrates with covalently linked ubiquitin chains in eukaryotes. Although proteasomes are distributed throughout the cell, specific biological functions of the proteasome in distinct subcellular locales remain largely unknown. We report that p...
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doaj-dde0d846a71d46af98bc81a56eaf42042020-11-25T02:03:27ZengElsevierCell Reports2211-12472013-07-0141193010.1016/j.celrep.2013.06.006The Ubiquitin Receptor S5a/Rpn10 Links Centrosomal Proteasomes with Dendrite Development in the Mammalian BrainSidharth V. Puram0Albert H. Kim1Hye-Yeon Park2Julius Anckar3Azad Bonni4Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USADepartment of Neurosurgery, Washington University School of Medicine, St. Louis, MO 63110, USADepartment of Neurobiology, Harvard Medical School, Boston, MA 02115, USADepartment of Neurobiology, Harvard Medical School, Boston, MA 02115, USADepartment of Neurobiology, Harvard Medical School, Boston, MA 02115, USA Proteasomes drive the selective degradation of protein substrates with covalently linked ubiquitin chains in eukaryotes. Although proteasomes are distributed throughout the cell, specific biological functions of the proteasome in distinct subcellular locales remain largely unknown. We report that proteasomes localized at the centrosome regulate the degradation of local ubiquitin conjugates in mammalian neurons. We find that the proteasomal subunit S5a/Rpn10, a ubiquitin receptor that selects substrates for degradation, is essential for proteasomal activity at centrosomes in neurons and thereby promotes the elaboration of dendrite arbors in the rodent brain in vivo. We also find that the helix-loop-helix protein Id1 disrupts the interaction of S5a/Rpn10 with the proteasomal lid and thereby inhibits centrosomal proteasome activity and dendrite elaboration in neurons. Together, our findings define a function for a specific pool of proteasomes at the neuronal centrosome and identify a biological function for S5a/Rpn10 in the mammalian brain. http://www.sciencedirect.com/science/article/pii/S2211124713002842 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sidharth V. Puram Albert H. Kim Hye-Yeon Park Julius Anckar Azad Bonni |
spellingShingle |
Sidharth V. Puram Albert H. Kim Hye-Yeon Park Julius Anckar Azad Bonni The Ubiquitin Receptor S5a/Rpn10 Links Centrosomal Proteasomes with Dendrite Development in the Mammalian Brain Cell Reports |
author_facet |
Sidharth V. Puram Albert H. Kim Hye-Yeon Park Julius Anckar Azad Bonni |
author_sort |
Sidharth V. Puram |
title |
The Ubiquitin Receptor S5a/Rpn10 Links Centrosomal Proteasomes with Dendrite Development in the Mammalian Brain |
title_short |
The Ubiquitin Receptor S5a/Rpn10 Links Centrosomal Proteasomes with Dendrite Development in the Mammalian Brain |
title_full |
The Ubiquitin Receptor S5a/Rpn10 Links Centrosomal Proteasomes with Dendrite Development in the Mammalian Brain |
title_fullStr |
The Ubiquitin Receptor S5a/Rpn10 Links Centrosomal Proteasomes with Dendrite Development in the Mammalian Brain |
title_full_unstemmed |
The Ubiquitin Receptor S5a/Rpn10 Links Centrosomal Proteasomes with Dendrite Development in the Mammalian Brain |
title_sort |
ubiquitin receptor s5a/rpn10 links centrosomal proteasomes with dendrite development in the mammalian brain |
publisher |
Elsevier |
series |
Cell Reports |
issn |
2211-1247 |
publishDate |
2013-07-01 |
description |
Proteasomes drive the selective degradation of protein substrates with covalently linked ubiquitin chains in eukaryotes. Although proteasomes are distributed throughout the cell, specific biological functions of the proteasome in distinct subcellular locales remain largely unknown. We report that proteasomes localized at the centrosome regulate the degradation of local ubiquitin conjugates in mammalian neurons. We find that the proteasomal subunit S5a/Rpn10, a ubiquitin receptor that selects substrates for degradation, is essential for proteasomal activity at centrosomes in neurons and thereby promotes the elaboration of dendrite arbors in the rodent brain in vivo. We also find that the helix-loop-helix protein Id1 disrupts the interaction of S5a/Rpn10 with the proteasomal lid and thereby inhibits centrosomal proteasome activity and dendrite elaboration in neurons. Together, our findings define a function for a specific pool of proteasomes at the neuronal centrosome and identify a biological function for S5a/Rpn10 in the mammalian brain.
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url |
http://www.sciencedirect.com/science/article/pii/S2211124713002842 |
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