Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction

Patrick Schreiner, Xiang Chen, Koraljka Husnjak, Leah Randles, Naixia Zhang, Suzanne Elsasser, Daniel Finley, Ivan Dikic (), Kylie J. Walters () and Michael Groll ()
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Patrick Schreiner: Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany
Xiang Chen: Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA
Koraljka Husnjak: Institute for Biochemistry II and Cluster of Excellence Macromolecular Complexes, Goethe University, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany
Leah Randles: Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA
Naixia Zhang: Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA
Suzanne Elsasser: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Daniel Finley: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Ivan Dikic: Institute for Biochemistry II and Cluster of Excellence Macromolecular Complexes, Goethe University, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany
Kylie J. Walters: Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA
Michael Groll: Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany

Nature, 2008, vol. 453, issue 7194, 548-552

Abstract: Proteasomes: Ubiquitin binding via Rpn 13 The 26S proteasome is a multisubunit complex that selectively degrades ubiquitin conjugated proteins. Two studies show that a known component of the proteasome, Rpn13 functions as a novel ubiquitin binding receptor. Structural studies reveal a novel mode of ubiquitin recognition. Rpn 13 is also a receptor for a deubiquitinating enzyme, suggesting a linkage between ubiquitin chain recognition and disassembly.

Date: 2008
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DOI: 10.1038/nature06924

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