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The ubiquitin receptor S5a/Rpn10 links centrosomal proteasomes with dendrite development in the mammalian brain.

Authors: Puram, SV  Kim, AH  Park, HY  Anckar, J  Bonni, A 
Citation: Puram SV, etal., Cell Rep. 2013 Jul 11;4(1):19-30. doi: 10.1016/j.celrep.2013.06.006. Epub 2013 Jul 3.
Pubmed: (View Article at PubMed) PMID:23831032
DOI: Full-text: DOI:10.1016/j.celrep.2013.06.006

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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CRRD Object Information
CRRD ID: 9686139
Created: 2015-02-03
Species: All species
Last Modified: 2015-02-03
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.