The COP9 Signalosome Inhibits p27kip1 Degradation and Impedes G1-S Phase Progression via Deneddylation of SCF Cul1

Xiaoming, Yang; Menon, Suchithra; Lykke-Andersen, Karin; Tsuge, Tomohiko; Xiao, Di; Wang, Xiping; Rodrı́guez-Suárez, Roberto; Zhang, Hui; Wei, Ning

doi:10.1016/s0960-9822(02)00791-1

Cited by 161 publications

(147 citation statements)

References 29 publications

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“…In support of this notion, recent studies using highly purified components showed that the CSN cleaved Nedd8 from hCUL1 catalytically . Additionally, in several organisms analysed (C. elegans, Drosophila and Arabidopsis), CSN activity is indispensable for deconjugation of Nedd8 from a number of tested cullins that include CUL1, CUL2 and CUL3 (Schwechheimer et al, 2001;Zhou et al, 2001;Yang et al, 2002;Doronkin et al, 2003;Pintard et al, 2003a). Surprisingly, requirement of the CSN for the deneddylation of spCUL4/Pcu4 might be different.…”

Section: Role Of Nedd8 Proteasesmentioning

confidence: 99%

“…e . f Schwechheimer et al, 2001;Cope et al, 2002;Yang et al, 2002;Doronkin et al, 2003;Lykke-Andersen et al, 2003;Pintard et al, 2003a;Wu et al, 2003;Yan et al, 2003). g (Mendoza et al, 2003;Wu et al, 2003) Role of Nedd8 in proteolysis Z-Q Pan et al…”

Section: Role Of Nedd8 Proteasesmentioning

confidence: 99%

“…Using in vitro assays, Yang et al (2002) have shown that the CSN inhibited p27 ubiquitination and degradation catalysed by HeLa cell cytosolic extracts. This inhibitory effect can be explained by the CSN deneddylase activity, which, by deconjugating Nedd8 from CUL1, is expected to reduce the SCF E3 ligase function.…”

Section: Role Of Nedd8 Proteasesmentioning

confidence: 99%

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Nedd8 on cullin: building an expressway to protein destruction

et al. 2004

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This review summarizes recent advances concerning the Nedd8 regulatory pathway in four areas. One, substantial progress has been made in delineating the role of cullin family proteins, the only known substrates of the Nedd8 modification system. Cullins are molecular scaffolds responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. Two, a large body of work has helped elucidate the molecular details underlying the Nedd8 modification reaction, which results in covalent conjugation of a Nedd8 moiety onto a conserved cullin lysine residue. Three, studies using a variety of genetic model systems have established an essential role for Nedd8 in cell cycle control and in embryogenesis by upregulating the activities of cullin-based E3 ligases. In vitro experiments have revealed a direct role for Nedd8 in activating ubiquitination. Construction of a model of the ROC1/ Rbx1-CUL1-Nedd8 structure suggests a mechanism by which the cullin-linked Nedd8 may assist the neighboring ROC1/Rbx1 in landing and positioning the E2 conjugating enzyme for the ubiquitin transfer reaction. Finally, increasing evidence indicates that removal of Nedd8 from its cullin targets, by the action of COP9 Signalosome and possibly other proteases, plays a significant role in the regulation of cullin-mediated proteolysis.

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Section: Role Of Nedd8 Proteasesmentioning

confidence: 99%

Section: Role Of Nedd8 Proteasesmentioning

confidence: 99%

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Nedd8 on cullin: building an expressway to protein destruction

et al. 2004

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“…The CSN has been found to possess an isopeptidase activity that removes RUB/NEDD8 from cullin [35]. Addition of the purified CSN complex to an in vitro p27 kip1 ubiquitination system inhibits p27 ubiquitination and degradation in a NEDDylation-dependent manner [36]. In Arabidopsis, a reduction in the level of the CSN results in increased levels of modified CUL1 and growth defects similar to the axr1 and rce1 mutants [35,37].…”

Section: Auxin Modulates Gene Transcriptionmentioning

confidence: 99%

Auxin signaling and regulated protein degradation

Dharmasiri

Estelle

2004

Trends in Plant Science

227

141

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Auxin regulates many aspects of plant growth and development. Auxin is known to regulate gene expression through degradation of the AUX/IAA proteins, short-lived nuclear proteins that regulate gene transcription. The AUX/IAA proteins are degraded through the action of a ubiquitin protein ligase called SCF TIR1 . Auxin promotes the interaction between AUX/IAA proteins and SCF TIR1 in a soluble extract, suggesting that the auxin receptor is a soluble factor. These studies also indicate that the auxin-induced AUX/IAA -SCF TIR1 interaction does not depend on phosphorylation or hydroxylation of AUX/IAA proteins. Although the mechanism of auxin-induced AUX/IAA -SCF TIR1 interaction is not yet clear, auxin might induce a modification in TIR1, AUX/IAA proteins or an adaptor protein that is required for the interaction.Auxin plays a pivotal role in many processes throughout the plant life cycle. These include embryogenesis, lateral root development, vascular differentiation, apical dominance, tropic responses and flower development. Auxin was first discovered decades ago [1]. In spite of the tremendous amount of information that has accumulated since then, the auxin signaling pathways have not been fully elucidated. Nevertheless, through the combined application of genetic, molecular and biochemical methods, we are beginning to understand some aspects of auxin action. In this article, we discuss recent developments in the study of auxin signaling, particularly focusing on auxin-regulated transcription.

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“…By native gel electrophoresis, Fukumoto et al, (2005) showed that CSN complexes are more dynamic and heterogeneous than previously believed. For example, the CSN5 subunit, also known as Jab1, can stably exist outside the CSN holocomplex (Kwok et al, 1998;Yang et al, 2002;Gusmaroli et al, 2004). Notably, the amount of the CSN5 populations outside of the CSN holocomplex can change in response to cellular environment and signaling cues (Fukumoto et al, 2005;Tomoda et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

CSN1 inhibits c-Jun phosphorylation and down-regulates ectopic expression of JNK1

et al. 2011

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CSN1 is a component of the COP9 signalosome (CSN), a conserved protein complex with pleiotropic functions in many organs and cell types. CSN regulates ubiquitinproteasome dependent protein degradation via the deneddylation and the associated deubiquitination activities. In addition, CSN associates with protein kinases and modulates cell signaling, particularly the activator protein 1 (AP-1) pathway. We have shown previously that CSN1 suppresses AP-1 transcription activity and inhibits ultraviolet (UV) and serum activation of c-fos expression. Here we show that CSN1 can inhibit phosphorylation of proto-oncogene c-Jun product and repress c-Jun dependent transcription. Further, CSN1 dramatically downregulates ectopic expression of c-Jun N-terminal kinase 1 (JNK1) in cultured cells. The decline in JNK1 is not caused by excessive proteolysis or by 3′ UTR-dependent mRNA instability, but by CSN1-dependent repression of one or multiple steps in transcriptional and posttranscriptional mechanisms. Thus, in contrast to CSN5/ Jab1, which promotes AP-1 activity, CSN1 displays a negative effect on the AP-1 pathway. Finally, we discuss about the dynamic equilibrium of the CSN complexes in regulation of the AP-1 pathway.

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The COP9 Signalosome Inhibits p27kip1 Degradation and Impedes G1-S Phase Progression via Deneddylation of SCF Cul1

Cited by 161 publications

References 29 publications

Nedd8 on cullin: building an expressway to protein destruction

Nedd8 on cullin: building an expressway to protein destruction

Auxin signaling and regulated protein degradation

CSN1 inhibits c-Jun phosphorylation and down-regulates ectopic expression of JNK1

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