Sci. STKE, 22 October 2002
Neddylation We're JAMMing
A protein motif termed JAMM has been identified that appears to be responsible for encoding a metallo-isopeptidase activity important in cleaving either ubiquitin or ubiquitin-like Nedd8 moieties from proteins (see the Perspective by Hochstrasser). Cope et al. show that in the COP9 signalosome, the JAMM motif acts to de-Neddylate substrates, such as those that are important in eye development. Verma et al. show that in the proteasome lid subcomplex, the JAMM motif is important in cleaving ubiquitin from a variety of substrates, and that inactivation of the JAMM motif is lethal in yeast.
G. A. Cope, G. S. B. Suh, L. Aravind, S. E. Schwarz, S. L. Zipursky, E. V. Koonin, R. J. Deshaies, Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1. Science 298, 608-611 (2002). [Abstract] [Full Text]
R. Verma, L. Aravind, R. Oania, W. H. McDonald, J. R. Yates, III, E. V. Koonin, R. J. Deshaies, Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611-615 (2002). [Abstract] [Full Text]
Citation: We're JAMMing. Sci. STKE 2002, tw384 (2002).
The editors suggest the following Related Resources on Science sites:
In Science Signaling
In Science Magazine
Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882