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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Main Authors: Sidharth V. Puram, Albert H. Kim, Hye-Yeon Park, Julius Anckar, Azad Bonni
Format: Article
Language:English
Published: Elsevier 2013-07-01
Series:Cell Reports
Online Access:http://www.sciencedirect.com/science/article/pii/S2211124713002842
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spelling 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.
url http://www.sciencedirect.com/science/article/pii/S2211124713002842
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