A New β-Catenin-dependent Activation Domain in T Cell Factor

Atcha, Fawzia A.; Munguia, Jesus E.; Li, Tony W.H.; Hovanes, Karine; Waterman, Marian L.

doi:10.1074/jbc.m213218200

Cited by 73 publications

(88 citation statements)

References 37 publications

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“…DGlut4EFd, Glut4EF, PBF, and ZNF704 also contain a CR domain at their C terminus that is highly similar to the transcriptional activation and DNA-binding domain present in E variants of the wingless/Wnt signaling effectors, TCF transcription factors (Arce et al 2006;Hoppler and Kavanagh 2007). In TCF, the CRARF domain is necessary for transcriptional activation mediated through both b-catenin and the CREB-binding protein (CBP)/p300 (Atcha et al 2003;Hecht and Stemmler 2003). This activity is important during development but its misregulation leads to overactive Wnt signaling and drives TCFs/lymphoid enhancing factors (LEFs) to transform cells (Arce et al 2006;Polakis 2007).…”

Section: Discussionmentioning

confidence: 99%

The Glucose Transporter (GLUT4) Enhancer Factor Is Required for Normal Wing Positioning in Drosophila

Yazdani

Huang

Terman³

2008

Genetics

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Many of the transcription factors and target genes that pattern the developing adult remain unknown. In the present study, we find that an ortholog of the poorly understood transcription factor, glucose transporter (GLUT4) enhancer factor (Glut4EF, GEF) ½also known as the Huntington's disease gene regulatory region-binding protein (HDBP) 1, plays a critical role in specifying normal wing positioning in adult Drosophila. Glut4EF proteins are zinc-finger transcription factors named for their ability to regulate expression of GLUT4 but nothing is known of Glut4EF's in vivo physiological functions. Here, we identify a family of Glut4EF proteins that are well conserved from Drosophila to humans and find that mutations in Drosophila Glut4EF underlie the wing-positioning defects seen in stretch mutants. In addition, our results indicate that previously uncharacterized mutations in Glut4EF are present in at least 11 publicly available fly lines and on the widely used TM3 balancer chromosome. These results indicate that previous observations utilizing these common stocks may be complicated by the presence of Glut4EF mutations. For example, our results indicate that Glut4EF mutations are also present on the same chromosome as two gain-of-function mutations of the homeobox transcription factor Antennapedia (Antp) and underlie defects previously attributed to Antp. In fact, our results support a role for Glut4EF in the modulation of morphogenetic processes mediated by Antp, further highlighting the importance of Glut4EF transcription factors in patterning and morphogenesis.

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Section: Discussionmentioning

confidence: 99%

The Glucose Transporter (GLUT4) Enhancer Factor Is Required for Normal Wing Positioning in Drosophila

Yazdani

Huang

Terman³

2008

Genetics

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“…In Figure 6A, the highly conserved WNT response elements downstream of Promoter 1 are indicated, as are the upstream AUGs and CUGs (Hovanes et al 2001;Atcha et al 2003). These WNT response elements activate Promoter 1 transcription as well as transcription of the weaker, internal Promoter 3 (data not shown; Atcha et al 2003).…”

Section: Discussionmentioning

confidence: 99%

An internal ribosome entry site mediates translation of lymphoid enhancer factor-1

Jiménez

Jang²,

Semler³

et al. 2005

RNA

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The lymphoid enhancer factor-1 LEF1 locus produces multiple mRNAs via alternative promoters. Full-length LEF-1 protein is produced via translation of an mRNA with a 1.2-kb, GC-rich 5 0 -untranslated region (UTR), whereas a truncated LEF-1 isoform is produced by an mRNA with a short, 60-nucleotide (nt) 5 0 -UTR. Full-length LEF-1 promotes cell growth via its interaction with the WNT signaling mediator b-catenin. Truncated LEF-1 lacks the b-catenin binding domain and opposes WNT signaling as a competitive inhibitor for WNT response elements. In this study we tested the hypothesis that the long, GC-rich 5 0 -UTR within the full-length LEF1 mRNA contains an internal ribosome entry site (IRES). Using a dicistronic vector in transient DNA transfections, we show that the LEF1 5 0 -UTR mediates cap-independent translation. Additional experiments involving a promoter-less dicistronic vector, Northern blot analysis, and transient transfections of dicistronic mRNAs into cultured mammalian cells compromised for cap-dependent translation demonstrate that the 5 0 -UTR of full-length LEF1 mRNA contains a bona fide IRES. Deletion analysis of the 5 0 -UTR shows that maximal IRES activity requires the majority of the 5 0 -UTR, consistent with the notion that cellular IRESs require multiple modules for efficient activity. This study demonstrates that full-length LEF1 mRNA has evolved to utilize a cap-independent mechanism for translation of full-length LEF-1, whereas the truncated isoform is produced via the canonical cap-dependent ribosome scanning mechanism.

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“…Like other TCF proteins, POP-1 has an amino-terminal catenin-binding domain through which it interacts with b-catenins BAR-1 and SYS-1, and an HMG box DNA-binding domain (Korswagen et al 2000;Natarajan et al 2001;Kidd et al 2005). It also possesses an extended carboxy-terminal tail (E tail) similar to that in alternatively spliced isoforms of human TCF1 and TCF4, which functions in auxiliary DNA-binding and protein -protein interactions (Atcha et al 2003(Atcha et al , 2007. Recent work suggests that this carboxy-terminal tail in POP-1 mediates the interaction with the b-catenin WRM-1 and results in phosphorylation of POP-1 and its nuclear export (Yang et al 2011) (see below).…”

Section: Tcf: There Can Be Only Onementioning

confidence: 99%