Proteasome subunit Rpn13 is a novel ubiquitin receptor

Koraljka Husnjak, Suzanne Elsasser, Naixia Zhang, Xiang Chen, Leah Randles, Yuan Shi, Kay Hofmann, Kylie J. Walters (), Daniel Finley () and Ivan Dikic ()
Additional contact information
Koraljka Husnjak: Institute of Biochemistry II and Cluster of Excellence Macromolecular Complexes, Goethe University, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany
Suzanne Elsasser: Harvard Medical School, 240 Longwood Avenue, Boston, Massachsuetts 02115, USA
Naixia Zhang: Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA
Xiang Chen: Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA
Leah Randles: Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA
Yuan Shi: Harvard Medical School, 240 Longwood Avenue, Boston, Massachsuetts 02115, USA
Kay Hofmann: Miltenyi Biotec GmbH, Stoeckheimer Weg 1, D-50829 Koeln, Germany
Kylie J. Walters: Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA
Daniel Finley: Harvard Medical School, 240 Longwood Avenue, Boston, Massachsuetts 02115, USA
Ivan Dikic: Institute of Biochemistry II and Cluster of Excellence Macromolecular Complexes, Goethe University, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany

Nature, 2008, vol. 453, issue 7194, 481-488

Abstract: Abstract Proteasomal receptors that recognize ubiquitin chains attached to substrates are key mediators of selective protein degradation in eukaryotes. Here we report the identification of a new ubiquitin receptor, Rpn13/ARM1, a known component of the proteasome. Rpn13 binds ubiquitin through a conserved amino-terminal region termed the pleckstrin-like receptor for ubiquitin (Pru) domain, which binds K48-linked diubiquitin with an affinity of approximately 90 nM. Like proteasomal ubiquitin receptor Rpn10/S5a, Rpn13 also binds ubiquitin-like (UBL) domains of UBL-ubiquitin-associated (UBA) proteins. In yeast, a synthetic phenotype results when specific mutations of the ubiquitin binding sites of Rpn10 and Rpn13 are combined, indicating functional linkage between these ubiquitin receptors. Because Rpn13 is also the proteasomal receptor for Uch37, a deubiquitinating enzyme, our findings suggest a coupling of chain recognition and disassembly at the proteasome.

Date: 2008
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DOI: 10.1038/nature06926

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