The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Promotion of NEDD8-CUL1 Conjugate Cleavage by COP9 Signalosome
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.
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Cited by
Function and regulation of cullin–RING ubiquitin ligases
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Multiple Associated Proteins Regulate Proteasome Structure and Function
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Ubiquitin, Hormones and Biotic Stress in Plants
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Metadata
- Authors
- Lyapina, S., Cope, G., Shevchenko, A., Serino, G., Tsuge, T., Zhou, C., Wolf, D. A., Wei, N., Shevchenko, A., & Deshaies, R. J.
- Venue
- Science
- Published
- 2001-05-18
- Volume
- 292
- Issue
- 5520
- Pages
- 1382-1385
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2003062513
- Cited by
- 698
- References
- 22
- FWCI
- 18.89
- Type
- journal article
- Language
- en
- Open access
- closed
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