Editor's Summary
22 May 2008
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.
News and Views: Cell biology: Two hands for degradation
Living cells must do away with regulatory proteins that are not needed. News comes of a considerable advance in understanding how the main agent of destruction, the proteasome, catches its targets.
Yasushi Saeki & Keiji Tanaka
doi:10.1038/453460a
Article: 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 & Ivan Dikic
doi:10.1038/nature06926
Abstract | Full Text | PDF (1,489K) | Supplementary information
Letter: 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 & Michael Groll
doi:10.1038/nature06924
First paragraph | Full Text | PDF (896K) | Supplementary information
