The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2

Kamura, Takumi; Conrad, Michael N.; Yan, Qin; Conaway, Ronald C.; Conaway, Joan Weliky

doi:10.1101/gad.13.22.2928

Cited by 252 publications

(209 citation statements)

References 25 publications

(37 reference statements)

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“…It has been published that the RING component of many CRL complexes, Rbx1, directly interacts with CSN6 in the CSN-CRL super-complexes [5,6]. Presumably Moreover, Rbx1 has been identified not only as a ubiquitinating enzyme in CRL complexes, but also as a ligase for Rub1, the yeast homolog of Nedd8 [40]. The decrease of neddylated proteins including Cul1 during apoptosis shown in Fig.…”

Section: Discussionmentioning

confidence: 95%

The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis

et al. 2007

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In concert with the ubiquitin (Ub) proteasome system (UPS) the COP9 signalosome (CSN) controls the stability of cellular regulators. The CSN interacts with cullin-RING Ub ligases (CRLs) consisting of a specific cullin, a RING protein as Rbx1 and substrate recognition proteins. The Ub-like protein Nedd8 is covalently linked to cullins and removed by the CSN-mediated deneddylation. Cycles of neddylation and deneddylation regulate CRLs. Apoptotic stimuli cause caspase-dependent modifications of the UPS.

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Section: Discussionmentioning

confidence: 95%

The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis

et al. 2007

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“…Early studies indicated that UBC12 can neddylate CUL1 in vitro in a manner that requires RBX1 [55][56][57] For simplicity, therefore, we refer to Cdc53 as yeast CUL1 throughout. This activity required the potentiating neddylation (PONY) domain of DCN1, which can interact with both the cullin and UBC12 [54,59].…”

Section: Mechanism Of Cullin Neddylationmentioning

confidence: 99%

“…Early studies indicated that UBC12 can neddylate CUL1 in vitro in a manner that requires RBX1 [55][56][57]. Genetic and biochemical data obtained initially in budding yeast and C. elegans, however, revealed that a novel conserved protein, DCN1, is necessary for maximum neddylation of yeast CUL1 orthologue Cdc53 in vitro and in vivo [58].…”

Section: Mechanism Of Cullin Neddylationmentioning

confidence: 99%

Building and remodelling Cullin–RING E3 ubiquitin ligases

2013

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Cullin-RING E3 ubiquitin ligases (CRLs) control a plethora of biological pathways through targeted ubiquitylation of signalling proteins. These modular assemblies use substrate receptor modules to recruit specific targets. Recent efforts have focused on understanding the mechanisms that control the activity state of CRLs through dynamic alterations in CRL architecture. Central to these processes are cycles of cullin neddylation and deneddylation, as well as exchange of substrate receptor modules to re-sculpt the CRL landscape, thereby responding to the cellular requirements to turn over distinct proteins in different contexts. This review is focused on how CRLs are dynamically controlled with an emphasis on how c ullin neddylation cycles are integrated with receptor exchange. Keywords: cullin; ubiquitin; Nedd8; COP9 signalosome; E3 ligase; CAND1 EMBO reports (2013) 14, 1050-1061 published online 15 November 2013; doi:10.1038/embor.2013 See the Glossary for abbreviations used in this article. IntroductionThe proteome is constantly remodelled to suit the needs of the cell, through both synthesis and turnover. Protein turnover is controlled through two main systems: the ubiquitin-proteasome system (UPS) and lysosomal degradation system, including autophagy. Although selective autophagy can provide a means by which to control the abundance of particular organelles and even single proteins, it is best understood as a means to control bulk turnover of cellular components [1]. Conversely, the UPS is a particularly versatile and highly regulated system [2] that allows selective turnover of individual regulatory proteins, even when they are incorporated into higher-order multiprotein assemblies. On the one hand, the entire population of a given protein targeted by the UPS might be subject to rapid tagging with ubiquitin and degradation by the proteasome. On the other hand, the UPS might control the degradation of only a small pool of a particular target protein, for example the population of a protein that has been phosphorylated by an upstream pathway. Thus, the UPS functions in space and time to sculpt the proteome and to control the abundance of active or inactive forms of signalling complexes and cellular machines. As illustrated in this Review, the UPS machinery that controls turnover of a wide swathe of the p roteome is itself dynamically regulated through many mechanisms.The tagging of proteins with particular types of ubiquitin chains serves to mark them for proteasomal degradation. This process occurs through an E1 (ubiquitin-activating enzyme)-E2 (ubiquitinconjugating enzyme)-E3 (ubiquitin ligase) cascade [3][4][5][6][7]. E3 plays a central role in substrate targeting by binding directly to the substrate and presenting target lysine residues to receive ubiquitin from the E2, in the case of RING E3s, or from a ubiquitin-charged cysteine residue in HECT and RBR E3s [6,[8][9][10]. Cullin-RING E3 ubiquitin ligases (CRLs), which were first discovered almost two decades ago [11][12][13], are a superfamily of RING E3...

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“…The Arabidopsis RUB E2 is called RCE (RUB-conjugating enzyme) and the Arabidopsis genome contains two RCE genes, RCE1 and RCE2 [14]. As for the RUB E3, recent studies suggest that the RBX1 protein functions as the E3 for RUB conjugation to CUL1 in Arabidopsis and budding yeast, and to human Cul2 [17,25,26]. The loss-of-function mutants axr1 and rce1 result in reduced CUL1 modification and consequent growth and development defects.…”

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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The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2

Cited by 252 publications

References 25 publications

The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis

The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis

Building and remodelling Cullin–RING E3 ubiquitin ligases

Auxin signaling and regulated protein degradation

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