Proteasome subunit Rpn13 is a novel ubiquitin receptor
Top Cited Papers
- 22 May 2008
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 453 (7194), 481-488
- https://doi.org/10.1038/nature06926
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. 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. The 26S proteasome is a multisubunit complex that selectively degrades ubiquitin conjugated proteins. Two studies (this Article and the Letter Dikic doi:10.1038/nature06924) show that a known component of the proteasome, Rpn13, functions as a novel ubiquitin binding receptor, and structural studies reveal a novel mode of ubiquitin recognition. Rpn13 is also a receptor for a deubiquitinating enzyme, suggesting a linkage between ubiquitin chain recognition and disassembly.Keywords
This publication has 37 references indexed in Scilit:
- Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interactionNature, 2008
- Ubiquitin Receptor Proteins hHR23a and hPLIC2 InteractJournal of Molecular Biology, 2007
- hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37The EMBO Journal, 2006
- A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomesThe EMBO Journal, 2006
- Analysis of the human protein interactome and comparison with yeast, worm and fly interaction datasetsNature Genetics, 2006
- Sem1p Is a Novel Subunit of the 26 S Proteasome from Saccharomyces cerevisiaeOnline Journal of Public Health Informatics, 2004
- Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysisBiochemical and Biophysical Research Communications, 2002
- A comprehensive two-hybrid analysis to explore the yeast protein interactomeProceedings of the National Academy of Sciences of the United States of America, 2001
- Interaction of hHR23 with S5aPublished by Elsevier BV ,1999
- Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasomeNature, 1997