A ubiquitin fusion reporter to monitor muscle proteostasis in C. elegans

Carl Elias Kutzner; Karen Carolyn Bauer; Thorsten Hoppe

doi:10.17912/micropub.biology.000824

A ubiquitin fusion reporter to monitor muscle proteostasis in C. elegans

MicroPubl Biol. 2023 Apr 21:2023:10.17912/micropub.biology.000824. doi: 10.17912/micropub.biology.000824. eCollection 2023.

Authors

Carl Elias Kutzner^{1

2

3}, Karen Carolyn Bauer^{1

2}, Thorsten Hoppe^{1

2

3}

Affiliations

¹ Institute for Genetics, University of Cologne, Cologne, Germany.
² Cologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases (CECAD), Cologne, Germany.
³ Center for Molecular Medicine (CMMC), Cologne, Germany.

Abstract

Muscle is a highly dynamic tissue in which a variety of folding and degradation processes are active to maintain protein homeostasis (proteostasis) and functionality. The muscle-specific chaperone UNC-45 folds the motor protein myosin and assembles it into myofilaments. Malfunction of this chaperone leads to misfolding of myosin, disorganization of myofilaments, and degradation of misfolded myosin molecules by the proteasome. Here, we present a new muscle-specific ubiquitin fusion degradation (UFD) model substrate in C. elegans that helps clarify how UNC-45 dysfunction affects muscle proteostasis.

Grants and funding

This work was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy – EXC 2030 – 390661388, FOR 2743, and by the European Research Council (ERC-CoG-616499) to T.H.