MSSP promotes ras/myc cooperative cell transforming activity by binding to c‐Myc

Niki, Takeshi; Izumi, Sachiyo; Saëgusa, Yumiko; Taira, Takahiro; Takai, Toshiki; Iguchi‐Ariga, Sanae M.M.; Ariga, Hiroyoshi

doi:10.1046/j.1365-2443.2000.00311.x

Cited by 45 publications

(55 citation statements)

References 48 publications

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“…The protein contains 2 RNA-binding domains and it can bind strongly to synthetic poly-U and poly-A oligoribonucleotides, suggesting that it is an RNAbinding protein (12). RBMS3 belongs to the family of c-Myc gene single-strand binding proteins (MSSP), which has 2 additional members, RBMS1 and RBMS2 (13,14). RBMS1 was reported to be involved in binding to c-Myc protein (14), but no such function has been described for RBMS3.…”

Section: Introductionmentioning

confidence: 99%

Downregulation of RBMS3 Is Associated with Poor Prognosis in Esophageal Squamous Cell Carcinoma

Chen

Nie

et al. 2011

Cancer Research

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Deletions on chromosome 3p occur often in many solid tumors, including esophageal squamous cell carcinoma (ESCC), suggesting the existence at this location of one or more tumor suppressor genes (TSG). In this study, we characterized RBMS3 gene encoding an RNA-binding protein as a candidate TSG located at 3p24. Downregulation of RBMS3 mRNA and protein levels was documented in approximately 50% of the primary ESCCs examined. Clinical association studies determined that RBMS3 downregulation was associated with poor clinical outcomes. RBMS3 expression effectively suppressed the tumorigenicity of ESCC cells in vitro and in vivo, including by inhibition of cell growth rate, foci formation, soft agar colony formation, and tumor formation in nude mice. Molecular analyses revealed that RBMS3 downregulated c-Myc and CDK4, leading to subsequent inhibition of Rb phosphorylation. Together, our findings suggest a tumor suppression function for the human RBMS3 gene in ESCC, acting through c-Myc downregulation, with genetic loss of this gene in ESCC contributing to poor outcomes in this deadly disease. Cancer Res; 71(19); 6106-15. Ó2011 AACR.

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Section: Introductionmentioning

confidence: 99%

Downregulation of RBMS3 Is Associated with Poor Prognosis in Esophageal Squamous Cell Carcinoma

Chen

Nie

et al. 2011

Cancer Research

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“…Since many candidate genes for transactivation have recently been identified by using the microarray method (7,8), identification of the bona fide target genes of c-Myc should be possible. For its versatile functions, c-Myc associates with various factors other than Max (5), including p107 (9, 10), TBP (11,12), Bin-1 (13), AMY-1 (14), TRRAP (15), PAM (16), ␣-tubulin (17), MM-1 (18), and Cdk inhibitor p21 (19), which bind to the N-proximal region of c-Myc, and also YY-1 (20), Miz-1 (21), AP2 (22), Nmi (23), BRCA1 (24), SNF5 (25), CBF-C/NF-YC (26), cdr2 (27), MSSP (28), CDC6 (29), and Orc1 (30), which bind to the Cproximal region. These binding proteins are thought to modulate c-Myc function, and mutation of the proteins or disregulated expression of their genes may lead to cell transformation by c-Myc.…”

mentioning

confidence: 99%

MM-1, a c-Myc-binding Protein, Is a Candidate for a Tumor Suppressor in Leukemia/Lymphoma and Tongue Cancer

Fujioka¹,

Taira²,

Maeda³

et al. 2001

Journal of Biological Chemistry

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The c-myc oncogene product (c-Myc) is a transcription factor that dimerizes with Max and recognizes the E-box sequence, and it plays key functions in cell proliferation, differentiation, and apoptosis. We previously showed that MM-1 bound to myc box II within the transactivation domain of c-Myc and repressed the E-box-dependent transcriptional activity of c-Myc. Here we report that MM-1 showed features of a tumor suppressor. In an EST data base search for cDNAs homologous to MM-1, we found a frequent substitution of amino acid 157 of MM-1, from alanine to arginine (A157R), and the substitution was observed more in tumor cells than in normal cells. A survey of the A157R mutation of MM-1 in 57 cultured cancer cells and 90 tissues from cancer patients showed that the A157R was present in about 50 -60% of leukemia/lymphoma cells and in more than 75% of squamous cell carcinoma of tongue cancer. Although both the A157R and the wild-type MM-1 bound to c-Myc, only A157R lost the activities to repress both the E-boxdependent transcriptional activity of c-Myc and the myc/ ras cooperative transforming activity in rat 3Y1 cells. Furthermore, the wild-type MM-1, but not A157R, arrested the growth of 3Y1 cells. The human MM-1 gene was mapped at chromosome 12q12-12q13, where many chromosome abnormalities in cancer cells have been reported. The results suggest that MM-1 is a novel candidate for a tumor suppressor that controls the transcriptional activity of c-Myc.

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“…Aliquots (2 mg) of the puri®ed GST-ORC1,5 or GSTwere ®rst applied to glutathione±Sepharose 4B (Amersham Pharmacia) in a buffer containing 20 mM Tris±HCl (pH 8.0), 150 mM NaCl, 0.5% NP-40 and 1 mM EDTA. The 0.1 mg of c-Myc released from MBP±c-Myc expressed in E. coli, as previously described (Taira et al 1999;Niki et al 2000), was then applied to the column. After extensive washing of the column with the same buffer as above, the proteins bound to the resin were recovered, separated in a 7.5% polyacrylamide gel containing SDS, blotted against an antic-Myc antibody (C-33, Santa Cruz), and detected by HRPconjugated anti-mouse Ig in an ECL system (Amersham Pharmacia).…”

Section: Methodsmentioning

confidence: 99%

“…These four proteins and full-size Max were expressed as fusion proteins of glutathione-Stransferase (GST) and af®nity-puri®ed by glutathione± Sepharose resin. Full-size c-Myc was ®rst expressed as a fusion protein of maltose-binding protein (MBP), and c-Myc was prepared after cleaving off MBP by PreScission protease as previously described (Taira et al 1999;Niki et al 2000). Then an in vitro binding assay, the so-called`pull-down assay', was carried out by incubating GST±ORCs and c-Myc under low (50 mM) or high (150 mM) salt conditions on glutathione±Se-pharose resin, and the bound protein(s) detected by Western blotting using an anti-c-Myc antibody (Fig.…”

Section: Interaction Of C-myc With Orc1mentioning

confidence: 99%

“…Proteins in the extract were ®rst immunoprecipitated with an anti-cMyc antibody or nonspeci®c IgG, and then the precipitates were blotted with an anti-T7 tag antibody. The speci®city of the anti-c-Myc antibody (C-33, Santa Cruz) used in this study was described previously (Niki et al 2000). The anti-c-Myc antibody, but not IgG, was 5).…”

Section: Complex Formation Between C-myc and Orcmentioning

confidence: 99%

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ORC1 interacts with c‐Myc to inhibit E‐box‐dependent transcription by abrogating c‐Myc–SNF5/INI1 interaction

et al. 2000

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Background: The c-myc oncogene product (c-Myc) is a transcription factor that forms a complex with Max and recognizes the E-box sequence. c-Myc plays key functions in cell proliferation, differentiation and apoptosis. As for its activity towards cell proliferation, it is generally thought that c-Myc transactivates the E-box-containing genes that encode proteins essential to cell-cycle progression. Despite the characterization of candidate genes regulated by c-Myc in culture cells, these have still not been ®rmly recognized as real target genes for cMyc.

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MSSP promotes ras/myc cooperative cell transforming activity by binding to c‐Myc

Cited by 45 publications

References 48 publications

Downregulation of RBMS3 Is Associated with Poor Prognosis in Esophageal Squamous Cell Carcinoma

Downregulation of RBMS3 Is Associated with Poor Prognosis in Esophageal Squamous Cell Carcinoma

MM-1, a c-Myc-binding Protein, Is a Candidate for a Tumor Suppressor in Leukemia/Lymphoma and Tongue Cancer

ORC1 interacts with c‐Myc to inhibit E‐box‐dependent transcription by abrogating c‐Myc–SNF5/INI1 interaction

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