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Published May 18, 2001 | Version Supplemental Material
Journal Article Open

Promotion of NEDD8-CUL1 Conjugate Cleavage by COP9 Signalosome

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Abstract

SCF ubiquitin ligases control various processes by marking regulatory proteins for ubiquitin-dependent proteolysis. To illuminate how SCF complexes are regulated, we sought proteins that interact with the human SCF component CUL1. The COP9 signalosome (CSN), a suppressor of plant photomorphogenesis, associated with multiple cullins and promoted cleavage of the ubiquitin-like protein NEDD8 from Schizosaccharomyces pombe CUL1 in vivo and in vitro. Multiple NEDD8-modified proteins uniquely accumulated in CSN-deficient S. pombe cells. We propose that the broad spectrum of activities previously attributed to CSN subunits—including repression of photomorphogenesis, activation of JUN, and activation of p27 nuclear export—underscores the importance of dynamic cycles of NEDD8 attachment and removal in biological regulation.

Additional Information

© 2001 American Association for the Advancement of Science. 12 February 2001; accepted 17 April 2001. Published Online May 3 2001. We thank C. Lois, J Roberts, T. Caspari, A. Carr, S. Forsburg, J. Thorner, T. Toda, F. Osaka, Y. Xiong, and P. Nurse for generously providing retroviral vectors, S. pombe strains, expression plasmids, and antibodies; M. Petroski for 32P-labeled ubiquitin; and R. Verma for experimental input, helpful discussions, and pointing out JAB1 homology to ubiquitin-specific proteases. We also thank P. Jackson and members of his laboratory for hosting this project in its early days. Supported by an Amgen fellowship (S.L.) and by the W. M. Keck Foundation and HHMI.

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Additional details

Identifiers

Eprint ID
51893
DOI
10.1126/science.1059780
Resolver ID
CaltechAUTHORS:20141118-095512539

Related works

Describes
10.1126/science.1059780 (DOI)

Funding

Amgen
W. M. Keck Foundation
Howard Hughes Medical Institute (HHMI)

Dates

Created
2014-11-18
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Updated
2021-11-10
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