The High-mobility Group Transcription Factor Sox10 Interacts with the N-myc-interacting Protein Nmi

Schlierf, Beate; Lang, Stefan; Kosian, Thomas; Werner, Torsten; Wegner, Michael

doi:10.1016/j.jmb.2005.09.013

Cited by 38 publications

(31 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…pCMV5-myc-Nmi was kindly provided by Beate Schlierf (Institut für Biochemie, Universität Erlangen-Nürnberg, Erlangen, Germany) (30), and the Nmi cDNA was subcloned into the pCMV-HA (Clontech, Mountain View, CA) and pCMV-Tag3B (Stratagene, La Jolla, CA) vectors. pCMV-HA-Nmi (tu) containing changes in nucleotides 340 to 345 from GTT GCT to GTG GCG, which did not change the amino acids of the Nmi protein, was generated using a QuikChange site-directed mutagenesis kit (Stratagene).…”

Section: Methodsmentioning

confidence: 99%

“…It contains an N-terminal coiledcoil domain (cc) followed by two tandem Nmi/IFP35 homology domains (NIDs). Nmi can interact with a variety of key transcription factors, such as c-Myc, N-Myc, Max, c-Fos, Sox-10, IFP35, apoptin, BRCA1, CKIP-1, and all signal transducer and activator of transcription (STAT) proteins except STAT2 (25)(26)(27)(28)(29)(30)(31)(32)(33). These protein-protein interactions suggest that Nmi is an important cytokine with various roles in multiple biological processes.…”

mentioning

confidence: 99%

See 1 more Smart Citation

N-Myc Interactor Inhibits Prototype Foamy Virus by Sequestering Viral Tas Protein in the Cytoplasm

Yang

Liu

et al. 2014

J Virol

View full text Add to dashboard Cite

Foamy viruses (FVs) are complex retroviruses that establish lifelong persistent infection without evident pathology. However, the roles of cellular factors in FV latency are poorly understood. This study revealed that N-Myc interactor (Nmi) could inhibit the replication of prototype foamy virus (PFV). Overexpression of Nmi reduced PFV replication, whereas its depletion by small interfering RNA increased PFV replication. The Nmi-mediated impairment of PFV replication resulted from the diminished transactivation by PFV Tas of the viral long terminal repeat (LTR) and an internal promoter (IP). Nmi was determined to interact with Tas and abrogate its function by sequestration in the cytoplasm. In addition, human and bovine Nmi proteins were found to inhibit the replication of bovine foamy virus (BFV) and PFV. Together, these results indicate that Nmi inhibits both human and bovine FVs by interfering with the transactivation function of Tas and may have a role in the host defense against FV infection. IMPORTANCEFrom this study, we report that the N-Myc interactor (Nmi), an interferon-induced protein, can interact with the regulatory protein Tas of the prototype foamy virus and sequester it in the cytoplasm. The results of this study suggest that Nmi plays an important role in maintaining foamy virus latency and may reveal a new pathway in the interferon-mediated antiviral barrier against viruses. These findings are important for understanding virus-host relationships not only with FVs but potentially for other retroviruses as well.

show abstract

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

N-Myc Interactor Inhibits Prototype Foamy Virus by Sequestering Viral Tas Protein in the Cytoplasm

Yang

Liu

et al. 2014

J Virol

View full text Add to dashboard Cite

show abstract

“…c-Myc, 2 N-Myc, 2,3 Max, 3 Sox-10, 4 IFP-35, 5,6 c-fos, 6 apoptin, 7 and all Stats except Stat2. 8 Nmi has also been demonstrated to interact with BRCA1, and block c-Myc induced human telomerase (hTERT) promoter activity.…”

mentioning

confidence: 99%

Nmi (N‐Myc interactor) inhibits Wnt/β‐catenin signaling and retards tumor growth

Fillmore

Mitra

et al. 2009

Intl Journal of Cancer

View full text Add to dashboard Cite

We found that the expression levels of N-Myc interactor (Nmi) were low in aggressive breast cancer cell lines when compared with less aggressive cell lines. However, the lower levels in the aggressive lines were inducible by interferon-gamma (IFN-gamma). Because Nmi has been reported to be a transcription cofactor that augments IFN-gamma induced transcription activity, we decided to test whether Nmi regulates expression of Dkk1, which is also inducible by IFN-gamma. We established stable clones constitutively expressing Nmi in MDA-MB-231 (breast) and MDA-MB-435 (melanoma) cell lines. Dkk1 was significantly up-regulated in the Nmi expressing clones concurrent with reduced levels of the critical transcription cofactor of Wnt pathway, beta-catenin. Treatment of the Nmi expressors with blocking antibody to Dkk1 restored beta-catenin protein levels. c-Myc is a known downstream target of activated beta-catenin signaling. Treatment of Nmi expressors with the proteosome inhibitor MG132, resulted in elevated beta-catenin levels with concomitant elevation of c-Myc levels. Our functional studies showed that constitutive expression of Nmi reduced the ability of tumor cells for the invasion, anchorage independent growth and tumor growth in vivo. Collectively, the data suggest that overexpression of Nmi inhibits the Wnt/beta-catenin signaling via up-regulation of Dkk1 and retards tumor growth.

show abstract

“…In contrast, Sox10 mutants that are unable to bind to DNA such as the WS095 mutation that carries an 30 Double-stranded oligonucleotides representing Cx47-D and Cx47-E from Connexin47 promoter 1b in their natural context (see Figure 5(a)) and C/C′ from the MPZ promoter 14 were used as probes. A larger DNA fragment spanning positions −82 to −21 of Connexin47 promoter 1b (Cx47-DE) was additionally employed.…”

Section: Activation Of Connexin47 Promoter 1b Requires Defined Sox10 mentioning

confidence: 99%

Expression of Connexin47 in Oligodendrocytes is Regulated by the Sox10 Transcription Factor

Schlierf

Werner

Glaser

et al. 2006

Journal of Molecular Biology

Self Cite

View full text Add to dashboard Cite

The High-mobility Group Transcription Factor Sox10 Interacts with the N-myc-interacting Protein Nmi

Cited by 38 publications

References 31 publications

N-Myc Interactor Inhibits Prototype Foamy Virus by Sequestering Viral Tas Protein in the Cytoplasm

N-Myc Interactor Inhibits Prototype Foamy Virus by Sequestering Viral Tas Protein in the Cytoplasm

Nmi (N‐Myc interactor) inhibits Wnt/β‐catenin signaling and retards tumor growth

Expression of Connexin47 in Oligodendrocytes is Regulated by the Sox10 Transcription Factor

Contact Info

Product

Resources

About