Critical Function for SIP, a Ubiquitin E3 Ligase Component of the β-Catenin Degradation Pathway, for Thymocyte Development and G1 Checkpoint

Fukushima, Toru; Zapata, Juán M.; Singha, Netai C.; Thomas, Michael; Kress, Christina L.; Krajewska, Maryla; Krajewski, Stan; Ronai, Ze’ev A.; Reed, John C.; Matsuzawa, Shu‐ichi

doi:10.1016/j.immuni.2005.12.002

Cited by 53 publications

(47 citation statements)

References 59 publications

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“…Our investigation on the behavior of these transfectants showed that a higher level of expression of CacyBP/SIP inhibited cell proliferation. On the contrary, reduction of CacyBP/SIP expression with RNA interference promoted cell growth, which was in accordance with the findings by Fukushima et al (6), that CacyBP/SIP-deficient mouse embryonic fibroblasts had a faster growth rate and showed enhanced proliferation properties. Furthermore, the overexpression of CacyBP/SIP suppressed the tumorigenicity of gastric cancer cells in vitro and relieved tumor malignant behavior in nude mice, whereas inhibition of CacyBP/SIP yielded the opposite effects.…”

Section: The Expression Of B-catenin In Transfectantssupporting

confidence: 91%

“…CacyBP/SIP is highly expressed in the mouse and in rat brain, liver, spleen, and stomach, and weakly in rat lung and kidney (4). Recent studies have suggested that CacyBP/SIP is implicated in the differentiation of erythroid cells, neurons, and rat neonatal cardiomyocytes (5), the development of thymocytes (6), and in mouse endometrial events, such as the establishment of pregnancy (7). It has been reported that the expression and translocation of CacyBP/SIP has been observed in neuroblastoma NB-2a cells (8).…”

Section: Introductionmentioning

confidence: 99%

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Calcyclin-Binding Protein Inhibits Proliferation, Tumorigenicity, and Invasion of Gastric Cancer

Ning¹,

Sun

Li³

et al. 2007

Molecular Cancer Research

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Calcyclin-binding protein/Siah-1 -interacting protein (CacyBP/SIP), a target protein of the S100 family, which includes S100A6, S100A1, S100A12, S100B, and S100P, has been identified as a component of a novel ubiquitinylation complex leading to B-catenin degradation. However, the function of CacyBP/SIP in gastric cancer has not been elucidated. In the present study, we prepared CacyBP/SIP overexpressing and knockdown cell lines of gastric cancer. Forced CacyBP/SIP expression inhibited the proliferation of gastric cancer cells, suppressed tumorigenicity in vitro, and prolonged the survival time of tumor-bearing nude mice. In addition, increased CacyBP/SIP repressed the invasive potential of gastric cancer cells. Conversely, the down-regulation of CacyBP/SIP by RNA interference showed the opposite effects. Further studies showed that depressed CacyBP/SIP increased the expression of total and nuclear B-catenin at the protein level and elevated the transcriptional activity of Tcf/LEF. Taken together, our results suggest that CacyBP/SIP may be a potential inhibitor of cell growth and invasion in the gastric cancer cell, at least in part through the effect on B-catenin protein expression and transcriptional activation of Tcf/LEF.

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Section: The Expression Of B-catenin In Transfectantssupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Calcyclin-Binding Protein Inhibits Proliferation, Tumorigenicity, and Invasion of Gastric Cancer

Ning¹,

Sun

Li³

et al. 2007

Molecular Cancer Research

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“…Previously, other members of S100A7 proteins such as S100A1, S100A6, S100A12, S100A7 inhibits SCCOC progression G Zhou et al S100B and S100P, were shown to interact with SIP in a calcium-dependent manner (Filipek et al, 2002). It remains to be determined whether S100A7 can also interact with SIP and participate in Siah-SIP-mediated b-catenin degradation as previously reported (Liu et al, 2001;Matsuzawa and Reed, 2001;Fukushima et al, 2006). Alternatively, S100A7 may target additional components of b-catenin-signaling or other important cell signaling pathways, which remain to be identified.…”

Section: Discussionmentioning

confidence: 80%

“…Because the degradation of b-catenin is controlled by a GSK3b-mediated phosphorylation-dependent (Hart et al, 1999;Kitagawa et al, 1999) (Moon et al, 2004;Willert and Jones, 2006) as well as Siah-1/Sip-mediated GSK3b phosphorylation-independent pathways (Liu et al, 2001;Matsuzawa and Reed, 2001;Fukushima et al, 2006), we used both luciferase assay and western blotting to test the possible mechanisms involved. As shown in Figure 4d, S100A7 did not appear to influence the activity of GSK3b, which regulates b-catenin levels by targeting it for degradation.…”

Section: S100a7 Inhibits Sccoc Progressionmentioning

confidence: 99%

Reciprocal negative regulation between S100A7/psoriasin and β-catenin signaling plays an important role in tumor progression of squamous cell carcinoma of oral cavity

et al. 2008

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Overexpression of S100A7 (psoriasin), a small calciumbinding protein, has been associated with the development of psoriasis and carcinomas in different types of epithelia, but its precise functions are still unknown. Using human tissue specimens, cultured cell lines, and a mouse model, we found that S100A7 is highly expressed in preinvasive, well-differentiated and early staged human squamous cell carcinoma of the oral cavity (SCCOC), but little or no expression was found in poorly differentiated, later-staged invasive tumors. Interestingly, our results showed that S100A7 inhibits both SCCOC cell proliferation in vitro and tumor growth/invasion in vivo. Furthermore, we demonstrated that S100A7 is associated with the b-catenin complex, and inhibits b-catenin signaling by targeting b-catenin degradation via a noncanonical mechanism that is independent of GSK3b-mediated phosphorylation. More importantly, our results also indicated that b-catenin signaling negatively regulates S100A7 expression. Thus, this reciprocal negative regulation between S100A7 and b-catenin signaling implies their important roles in tumor development and progression. Despite its high levels of expression in early stage SCCOC tumorigenesis, S100A7 actually inhibits SCCOC tumor growth/invasion as well as tumor progression. Downregulation of S100A7 in later stages of tumorigenesis increases b-catenin signaling, leading to promotion of tumor growth and tumor progression.

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“…23 Calcyclinbinding protein (SIP) as a ubiquitin E3 ligase component of the p53-induced b-catenin degradation pathway functions as an essential checkpoint for cell-cycle progression. 24 CDKN1A binds to and inhibits the activity of cyclin-CDK2 or -CDK4 complexes to induce G 1 -phase arrest. 25,26 GADD45-b negatively regulates cell growth by interacting with cdc2 and cyclin B, thus causing G 2 /M cell-cycle arrest.…”

Section: Effects On Cell Growth and Deathmentioning

confidence: 99%

Genomic view of IFN-α response in pre-autoimmune NZB/W and MRL/lpr mice

Shen

et al. 2007

Genes Immun

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Interferon (IFN)-a is involved in the pathogenesis of systemic lupus erythematosus. Studies in murine lupus models have revealed that type I IFN exerts either a protective effect in MRL/lpr, or can detrimentally impact disease progression, as in NZB/ W mice. To understand this paradox, we examined the kinetic global gene expression in pre-autoimmune NZB/W-, MRL/lprand normal BALB/c-derived splenic mononuclear cells following ex vivo IFN-a treatment. Analysis of IFN-a-induced gene expression patterns revealed genes associated with antiproliferative activity of IFN-a including CDKN1A, GADD45B, pituitary tumor-transforming 1, SCOTIN, ataxia telangiectasia-mutated homolog and calcyclin-binding protein were upregulated in MRL/ lpr and/or BALB/c mice. Of IFN-a-induced genes differentially expressed in NZB/W vs BALB/c and MRL/lpr mice at 3 h time point, enhanced expression of CCND1, cyclin D2, matrix metalloproteinase 13 and a panel of cytokines and chemokines and impaired expression of negative inflammatory regulators CD69 and an Src family kinase hemopoietic cell kinase were notable. Interestingly, the splenic mononuclear cells from the NZB/W not MRL/lpr lupus-prone mice at the pre-autoimmune stage before ex vivo IFN-a treatment, have increased expression of many known IFN-regulated genes. These results provide a unique genomic view of ex vivo IFN-a response in two lupus-prone models, and help to have an insight into the role of IFN-a in lupus pathogenesis Genes and Immunity (2007) IntroductionSystemic lupus erythematosus (SLE) is a prototypic systemic autoimmune disease characterized by a break of immune tolerance to self antigens, resulting in inflammation and damage to a range of organ systems. The exact pathoetiology of SLE remains elusive. Elevated serum levels of IFN-a have long been observed and correlated with disease activity. A series of studies using microarray gene expression analysis in patient peripheral blood cells demonstrated an 'IFN signature' in SLE, which correlated with renal and hematological involvement of phenotypes. [1][2][3][4][5][6] Supporting evidence has also come from studies on murine lupus. The (New Zealand Black (NZB) Â New Zealand White (NZW))F1 hybrid female mice (NZB/W) develop a disease closely resembling human SLE, characterized by the production of antinuclear antibodies, severe glomerulonephritis and early mortality. In the NZB parental strain, which also develops a lupus-like syndrome, homozygous IFN-a/b R-deleted NZB mice had significantly reduced antierythrocyte autoantibodies, erythroblastosis, hemolytic anemia, anti-DNA autoantibodies, kidney disease and mortality. 7 In contrast to normal BALB/c mice, continuous in vivo treatment of IFN-a in pre-autoimmune NZB/W mice from 8 weeks of age precipitates the autoimmune process and kidney damage, leading to premature death from severe immune complex glomerulonephritis. This result provides a direct evidence that IFN-a is implicated in the pathogenesis of SLE. 8 Thus, the type I IFNs have emerged as a dominant target in the path...

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Critical Function for SIP, a Ubiquitin E3 Ligase Component of the β-Catenin Degradation Pathway, for Thymocyte Development and G1 Checkpoint

Cited by 53 publications

References 59 publications

Calcyclin-Binding Protein Inhibits Proliferation, Tumorigenicity, and Invasion of Gastric Cancer

Calcyclin-Binding Protein Inhibits Proliferation, Tumorigenicity, and Invasion of Gastric Cancer

Reciprocal negative regulation between S100A7/psoriasin and β-catenin signaling plays an important role in tumor progression of squamous cell carcinoma of oral cavity

Genomic view of IFN-α response in pre-autoimmune NZB/W and MRL/lpr mice

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