Involvement of Bag6 and the TRC pathway in proteasome assembly

Takashi Akahane, Kazutaka Sahara, Hideki Yashiroda, Keiji Tanaka and Shigeo Murata ()
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Takashi Akahane: Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo
Kazutaka Sahara: Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo
Hideki Yashiroda: Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo
Keiji Tanaka: Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science
Shigeo Murata: Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo

Nature Communications, 2013, vol. 4, issue 1, 1-8

Abstract: Abstract The 26S proteasome has an elaborate structure, consisting of 33 different subunits that form the 20S core particle capped by the 19S regulatory particle on either end. Several chaperones that are dedicated to the accurate assembly of this protease complex have been identified, but the mechanisms underlying proteasome biogenesis remain unexplored so far. Here we report that core particle assembly becomes less efficient if the TRC pathway, which mediates insertion of tail-anchored proteins, is defective. We demonstrate that Bag6, a protein in the TRC pathway that is also responsible for the degradation of mislocalized proteins, is not only involved in core particle assembly but also has a key role in efficient regulatory particle assembly by directly associating with precursor regulatory particles. These findings indicate that proteasome assembly is not solely mediated by dedicated chaperones but also depends on general chaperones that preserve protein homeostasis.

Date: 2013
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DOI: 10.1038/ncomms3234

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