UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins

Doris Hellerschmied, Max Roessler, Anita Lehner, Linn Gazda, Karel Stejskal, Richard Imre, Karl Mechtler, Alexander Dammermann () and Tim Clausen ()
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Doris Hellerschmied: Vienna BioCenter (VBC)
Max Roessler: University of Vienna
Anita Lehner: Doktor-Bohr-Gasse 3
Linn Gazda: Vienna BioCenter (VBC)
Karel Stejskal: Vienna BioCenter (VBC)
Richard Imre: Vienna BioCenter (VBC)
Karl Mechtler: Vienna BioCenter (VBC)
Alexander Dammermann: University of Vienna
Tim Clausen: Vienna BioCenter (VBC)

Nature Communications, 2018, vol. 9, issue 1, 1-15

Abstract: Abstract Muscle development requires the coordinated activities of specific protein folding and degradation factors. UFD-2, a U-box ubiquitin ligase, has been reported to play a central role in this orchestra regulating the myosin chaperone UNC-45. Here, we apply an integrative in vitro and in vivo approach to delineate the substrate-targeting mechanism of UFD-2 and elucidate its distinct mechanistic features as an E3/E4 enzyme. Using Caenorhabditis elegans as model system, we demonstrate that UFD-2 is not regulating the protein levels of UNC-45 in muscle cells, but rather shows the characteristic properties of a bona fide E3 ligase involved in protein quality control. Our data demonstrate that UFD-2 preferentially targets unfolded protein segments. Moreover, the UNC-45 chaperone can serve as an adaptor protein of UFD-2 to poly-ubiquitinate unfolded myosin, pointing to a possible role of the UFD-2/UNC-45 pair in maintaining proteostasis in muscle cells.

Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-02924-7

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DOI: 10.1038/s41467-018-02924-7

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