Journal
NATURE
Volume 453, Issue 7194, Pages 481-488Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature06926
Keywords
-
Categories
Funding
- NCI NIH HHS [R01 CA097004, CA097004, R01 CA097004-06A1, R01 CA097004-05] Funding Source: Medline
- NIGMS NIH HHS [GM008700, T32 GM008700, R37 GM043601-17, R01 GM043601, R37 GM043601, T32 GM008700-09, GM043601] Funding Source: Medline
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available