The Emerging Role of the COP9 Signalosome in Cancer

Richardson, Katharine S.; Zundel, Wayne

doi:10.1158/1541-7786.mcr-05-0233

Cited by 99 publications

(90 citation statements)

References 110 publications

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“…As for PIF3, the light-specific phosphorylation forms of PIF4 and PIF5 appear to be the shortest-lived ones (Figures 4 and 6). Regulation of proteasome-mediated degradation of transcription factors is not uncommon (AlSady et al, 2006;Collins and Tansey, 2006;Hardtke et al, 2000;Richardson and Zundel, 2005). In mammalian systems, activation and degradation of transcription factors are often coupled, presumably to ensure tight control of the activation mechanism (Collins and Tansey, 2006).…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, in response to a light treatment, additional more slowly-migrating forms appear very transiently (Figures 4-6, and Supplementary Figures S2 and S3). As proteasomemediated degradation is often regulated by specific phosphorylation events (Al-Sady et al, 2006;Collins and Tansey, 2006;Hardtke et al, 2000;Richardson and Zundel, 2005), we tested whether PIF4 and PIF5 are phosphoproteins. Extracts of dark-grown and etiolated seedlings exposed for 1 h to R Figure 6.…”

Section: Pif5 Protein Accumulation Is Controlled By R/fr Ratiomentioning

confidence: 99%

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Phytochrome‐mediated inhibition of shade avoidance involves degradation of growth‐promoting bHLH transcription factors

Lorrain¹,

Allen²,

Duek³

et al. 2007

The Plant Journal

682

848

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SummaryPlant growth and development are particularly sensitive to changes in the light environment and especially to vegetational shading. The shade-avoidance response is mainly controlled by the phytochrome photoreceptors. In Arabidopsis, recent studies have identified several related bHLH class transcription factors (PIF, for phytochrome-interacting factors) as important components in phytochrome signaling. In addition to a related bHLH domain, most of the PIFs contain an active phytochrome binding (APB) domain that mediates their interaction with light-activated phytochrome B (phyB). Here we show that PIF4 and PIF5 act early in the phytochrome signaling pathways to promote the shade-avoidance response. PIF4 and PIF5 accumulate to high levels in the dark, are selectively degraded in response to red light, and remain at high levels under shademimicking conditions. Degradation of these transcription factors is preceded by phosphorylation, requires the APB domain and is sensitive to inhibitors of the proteasome, suggesting that PIF4 and PIF5 are degraded upon interaction with light-activated phyB. Our data suggest that, in dense vegetation, which is rich in far-red light, shade avoidance is triggered, at least partially, as a consequence of reduced phytochrome-mediated degradation of transcription factors such as PIF4 and PIF5. Consistent with this idea, the constitutive shadeavoidance phenotype of phyB mutants partially reverts in the absence of PIF4 and PIF5.

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Section: Discussionmentioning

confidence: 99%

Section: Pif5 Protein Accumulation Is Controlled By R/fr Ratiomentioning

confidence: 99%

Phytochrome‐mediated inhibition of shade avoidance involves degradation of growth‐promoting bHLH transcription factors

Lorrain¹,

Allen²,

Duek³

et al. 2007

The Plant Journal

682

848

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“…Taken together, our data suggest that Rig-G may work as a negative regulator of JAB1 function. Over the last several years, JAB1 also has been known as COP9 signalosome subunit 5 (CSN5), which is a component of the COP9 signalosome regulatory complex (26)(27)(28). Some reports show that JAB1͞CSN5 subunit possesses a metalloprotease catalytic activity that is required for the COP9 holocomplexdirected deneddylation of the Cullins, a subunit of SCF (Skp1-Cullin-F-box protein) ubiquitin E3 ligases (29,30).…”

Section: Discussionmentioning

confidence: 99%

“…Some reports show that JAB1͞CSN5 subunit possesses a metalloprotease catalytic activity that is required for the COP9 holocomplexdirected deneddylation of the Cullins, a subunit of SCF (Skp1-Cullin-F-box protein) ubiquitin E3 ligases (29,30). Although JAB1͞CSN5 can exist in a monomeric form and act independently of COP9 holocomplex (7,28), it should be interesting to explore in the future whether Rig-G has effects on the function of COP9 holocomplex through interaction with JAB1͞CSN5.…”

Section: Discussionmentioning

confidence: 99%

RIG-G as a key mediator of the antiproliferative activity of interferon-related pathways through enhancing p21 and p27 proteins

Xiao

Liu

Zhu

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

110

113

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The RIG-G gene, originally isolated from an acute promyelocytic leukemia cell line NB4, codes for a 60-kDa cytoplasmic protein that is induced by all-trans retinoic acid (ATRA) treatment along with the induction of morphological differentiation of NB4 cells. Here, we provide evidence that ectopic expression of Rig-G in U937 cells can lead to a significant accumulation of cells at G 1͞S transition. Growth arrest seems to occur by modulating several major cell cycle regulatory players. Interestingly, Rig-G alters JAB1 cellular distribution through interacting with this protein and increases the intracellular level of p27 by preventing it from the JAB-1-dependent and ubiquitin͞proteasome-mediated degradation. Furthermore, we demonstrate a role of Rig-G for c-myc down-regulation that results in an up-regulation of p21, tightly associated with cell cycle arrest. In addition, our studies reveal that Rig-G is a direct target of STAT1, a key transcription factor in regulating IFN responses, and may be one of the first experimentally proven molecular mediators for the antiproliferative effect of IFN-␣. Considering that IFN-␣ and ATRA synergistically inhibit growth along the intracellular pathways triggered by the two compounds in many cell types, we suggest that Rig-G may also represent one of the key molecular nodes of signaling cross-talk between ATRA and IFN-␣.cell growth inhibition ͉ retinoic acid ͉ Rig-G ͉ STAT1

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“…This both terminates E3 activity and is required for the reassembly of new CRLs (Wei et al, 2008). The CSN plays a role in many cancer-associated pathways including the cell cycle and DNA damage repair, and both CSN and CRL components may be dysregulated in tumours (Richardson and Zundel, 2005). Ubp12p, an S. pombe ortholog of human USP15, was shown through a systematic mass spectrometry screen to bind the CSN (Zhou et al, 2003).…”

Section: Functionmentioning

confidence: 99%

USP15 (ubiquitin specific peptidase 15)

Faronato¹,

Urbé²,

Coulson³

2012

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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IdentityOther names: KIAA0529; UNPH4; Unph-2 HGNC (Hugo): USP15 Location: 12q14.1 DNA/RNANote USP15 is a member of the ubiquitin-specific protease (USP) family; these cysteine proteases comprise the largest sub-group of deubiquitinase enzymes (DUBs). USP15 cleaves the isopeptide bonds of polyubiquitin chains, and can cleave linear ubiquitin fusion proteins (Baker et al., 1999). DescriptionThe USP15 gene spans 145 kb of genomic DNA. TranscriptionFour transcripts of the human USP15 gene are described by Ensembl and are summarized in the accompanying diagram and table. According to Entrezgene, USP15 encodes a single reference sequence mRNA of 4611bp (NM_006313.1) composed of 21 exons, which corresponds to USP15-203. However, three other USP15 splice variants utilise several alternative-splicing sites between exon 5 and exon 7 of this reference sequence. USP15-201, a 4698 bp mRNA comprised of 22 exons, is expressed at similar levels to the reference sequence (Angelats et al., 2003). Expression of the remaining variants, USP15-204 and the truncated USP15-202, is less well studied.Schematic illustrating four human USP15 transcripts. The USP15 reference sequence mRNA (USP15-203) and three alternative splice variants are illustrated. The approximate position and size of exons within the USP15 gene, according to Ensembl, is shown for each splice variant. Schematic illustrating four human USP15 isoforms. The domain structure is shown for the reference sequence protein (USP15-203) and three alternative isoforms according to Ensembl. DUSP, domain present in ubiquitin-specific proteases; UBL, ubiquitin-like fold; UCH, ubiquitin carboxyl-terminal hydrolase. The cysteine motifs that form the zinc-binding site are shown in purple and the amino acids comprising the catalytic triad are shown in red. The approximate location of nuclear export sequences (triangles) and a putative nuclear localisation signal (inverted triangle) are shown above isoform USP15-203. Differences in amino acid sequence between isoforms are shown in light blue. The UCH is absent in isoform USP15-202, but USP15-201, USP15-203 and USP15-204 are predicted to be catalytically active. USP15 (ubiquitin specific peptidase 15)

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The Emerging Role of the COP9 Signalosome in Cancer

Cited by 99 publications

References 110 publications

Phytochrome‐mediated inhibition of shade avoidance involves degradation of growth‐promoting bHLH transcription factors

Phytochrome‐mediated inhibition of shade avoidance involves degradation of growth‐promoting bHLH transcription factors

RIG-G as a key mediator of the antiproliferative activity of interferon-related pathways through enhancing p21 and p27 proteins

USP15 (ubiquitin specific peptidase 15)

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