DeNeddylation

The most studied function of the CSN is the regulation of protein degradation through deneddylation of the cullin subunit of cullin-based E3-ubiquitin ligases. The CSN removes Nedd8 —a ubiquitin-like modifier— from cullin-based E3 ubiquitin ligases (1), thereby regulating ligase activity. The deneddylation activity resides in the JAMM/MPN+ domain of CSN5 (2)MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function. BMC Biochem 3, 28.">(3), and the intact complex is necessary and sufficient for deneddylation (4).

-- DannyC - 30 May 2010

Notes

1 : Lyapina, S., Cope, G., Shevchenko, A., Serino, G., Tsuge, T., Zhou, C., Wolf, D.A., Wei, N., and Deshaies, R.J. (2001). Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome. Science 292, 1382-1385.

2 : Cope, G.A., Suh, G.S., Aravind, L., Schwarz, S.E., Zipursky, S.L., Koonin, E.V., and Deshaies, R.J. (2002). Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of NEDD8 from CUL1. Science 15, 15.

3 : Maytal-Kivity, V., Reis, N., Hofmann, K., and Glickman, M.H. (2002). MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function. BMC Biochem 3, 28.

4 : Enchev, R. I., Schreiber, A., Beuron, F., Morris, E. P. (2010) Structural Insights into the COP9 Signalosome and Its Common Architecture with the 26S Proteasome Lid and eIF3. STRUCTURE, 18 (4). pp. 518-527.


r1 - 30 May 2010 - 16:01:14 - DannyC
This site is powered by the TWiki collaboration platformCopyright © 2008-2014 by the contributing authors. All material on this collaboration platform is the property of the contributing authors.
Ideas, requests, problems regarding TWiki? Send feedback
Syndicate this site RSSATOM