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C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation

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  • Christian Heinen

    (Karolinska Institutet, von Eulers väg 3
    Present address: Department of Molecular and Cellular Biology, Harvard University, Northwest Building, Cambridge, Massachusetts 02138, USA.)

  • Klàra Ács

    (Karolinska Institutet, von Eulers väg 3)

  • Deborah Hoogstraten

    (Karolinska Institutet, von Eulers väg 3)

  • Nico P. Dantuma

    (Karolinska Institutet, von Eulers väg 3)

Abstract

The ubiquitin receptors Rad23 and Dsk2 deliver polyubiquitylated substrates to the proteasome for destruction. The C-terminal ubiquitin-associated (UBA) domain of Rad23 functions as a cis-acting stabilization signal that protects this protein from proteasomal degradation. Here, we provide evidence that the C-terminal UBA domains guard ubiquitin receptors from destruction by preventing initiation of degradation at the proteasome. We show that introduction of unstructured polypeptides that are sufficiently long to function as initiation sites for degradation abrogates the protective effect of UBA domains. Vice versa, degradation of substrates that contain an unstructured extension can be attenuated by the introduction of C-terminal UBA domains. Our study gains insight into the molecular mechanism responsible for the protective effect of UBA domains and explains how ubiquitin receptors can shuttle substrates to the proteasome without themselves becoming subject to proteasomal degradation.

Suggested Citation

  • Christian Heinen & Klàra Ács & Deborah Hoogstraten & Nico P. Dantuma, 2011. "C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation," Nature Communications, Nature, vol. 2(1), pages 1-9, September.
    • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1179
    DOI: 10.1038/ncomms1179
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