cul-1 Is Required for Cell Cycle Exit in C. elegans and Identifies a Novel Gene Family

Kipreos, Edward T.; Lander, Lois E; Wing, John P.; He, Wei; Hedgecock, Edward M.

doi:10.1016/s0092-8674(00)81267-2

Cited by 419 publications

(381 citation statements)

References 40 publications

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“…J.R.L. is a Damon Runyon Fellow supported by the Damon Runyon Cancer Research (DRG 2061-10 EM (1996) cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family. …”

Section: Acknowledgementsmentioning

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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Section: Acknowledgementsmentioning

confidence: 99%

Building and remodelling Cullin–RING E3 ubiquitin ligases

2013

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“…The other two cullin homologous genes were designated pcu3 þ (SPAC24H6.03) and pcu4 þ (SPAC3 A11) as the predicted products of the two genes showed the highest homology to cullin-3 and cullin-4, respectively (42% and 40%, respectively, Kipreos et al 1996). Budding yeast contains, in addition to Cdc53, two ORFs which are cullin members.…”

Section: Cullin Homologues In the Fission Yeast Genomementioning

confidence: 99%

“…Cdc53 acts as a scaffold for the SCF complex (Patton et al 1998a) and is also conserved. Furthermore, Cdc53 comprises a large protein family called cullin (Cdc53 is a cullin-1 homologue and humans have at least six cullin members, Kipreos et al 1996).…”

Section: Introductionmentioning

confidence: 99%

Two F‐box/WD‐repeat proteins Pop1 and Pop2 form hetero‐ and homo‐complexes together with cullin‐1 in the fission yeast SCF (Skp1‐Cullin‐1‐F‐box) ubiquitin ligase

1998

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“…Quite recently, we reported that a major target of NEDD8-ylation is Hs-Cul-4A (Osaka et al, 1998), but it has been reported so far that human cullins consist of six family proteins termed Cul-1, Cul-2, Cul-3, Cul-4A, Cul-4B, and Cul-5 (Kipreos et al, 1996). It remains obscure whether NEDD8 is also ligated to other Hs-Cul-family proteins in addition to Cul-4A.…”

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confidence: 99%

Covalent modification of all members of human cullin family proteins by NEDD8

et al. 1999

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Recently we found that NEDD8, a ubiquitin-like protein, was linked covalently to human cullin-4A (abbreviated Cul-4A) by a new ubiquitin-related pathway that is analogous to but distinct from the ligating system for SUMO1, another ubiquitin-like protein. However, it remained unknown whether the other ®ve members of the family of human cullin/Cdc53 proteins are modi®ed by NEDD8. Here we report that all Hs-Cul family proteins, such as Cul-1, Cul-2, Cul-3, Cul-4B, and Cul-5, in addition to Cul-4A, were modi®ed by covalent attachment of NEDD8 in rabbit reticulocyte lysates. Moreover, by comprehensive Northern-blot analyses, we examined multiple tissue distributions of the messages for all Cul-family proteins, NEDD8, and the NEDD8-ligating system consisting of APP-BP1/hUba3, and hUbc12, which function as E1-and E2-like enzymes, respectively. The expressions of Cul-1, Cul-2, and Cul-3 resembled each other and were apparently correlated to those of NEDD8 and the NEDD8-ligating system in various human cells and tissues. However, the mRNA levels of Cul-4A, Cul-4B, and Cul-5 di ered considerably from each other as well as from other Cul-family proteins. The enhanced expression of all Cul-family proteins except Cul-5 was observed in a variety of tumor cell lines.

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cul-1 Is Required for Cell Cycle Exit in C. elegans and Identifies a Novel Gene Family

Cited by 419 publications

References 40 publications

Building and remodelling Cullin–RING E3 ubiquitin ligases

Building and remodelling Cullin–RING E3 ubiquitin ligases

Two F‐box/WD‐repeat proteins Pop1 and Pop2 form hetero‐ and homo‐complexes together with cullin‐1 in the fission yeast SCF (Skp1‐Cullin‐1‐F‐box) ubiquitin ligase

Covalent modification of all members of human cullin family proteins by NEDD8

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