eyelidantagonizes wingless signaling during Drosophiladevelopment and has homology to the Bright family of DNA-binding proteins

Treisman, Jessica E.; Luk, Alvin; Rubin, Gerald M.; Heberlein, Ulrike

doi:10.1101/gad.11.15.1949

Cited by 98 publications

(120 citation statements)

References 108 publications

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“…Mutations in brm, snr1, and osa all affect eye development (Treisman et al 1997;Brumby et al 2002;Marenda et al 2003), and mutations in the trithorax genes trithorax, brahma, kohtalo, and skuld were recently identified in a mosaic genetic screen used to identify genes required for retinal patterning ( Janody et al 2004). Our identification of kis in our genetic screen led us to hypothesize that other trithorax group genes might also be involved in regulating Atonal expression.…”

Section: Ao9mentioning

confidence: 93%

“…Further, many of the trithorax genes required for specific cellular processes in the eye have a ubiquitous expression pattern in the eye (Kuzin et al 1994;Treisman et al 1997;Janody et al 2003;Zraly et al 2003), much like the Kismet protein. This expression data might suggest a dynamic functional and developmental regulation of these factors.…”

Section: Discussionmentioning

confidence: 99%

“…BL number refers to Bloomington Stock Center stock number. Stocks used: ato 1090 (also called ato ts , described here), Df(3R)p13 [BL 1943 ato 1 and ato 3 ( Jarman et al 1994( Jarman et al , 1995], atonal-lacZ enhancer trap lines (both 59F:9.3 and 39F:5.8) are described in Sun et al (1998), hh AC (Lee et al 1992), Egfr E1 Rubin 1989, 1992), lilli XS407 (gift from Amy Tang) (Tang et al 2001), lilli XS575 (gift from Amy Tang) (Tang et al 2001), lilli A17-2 (gift from Arno Muller) (Muller et al 2005), lilli S35 (Neufeld et al 1998a), kis 1 (Kennison and Tamkun 1988), kis k13416 (Roch et al 1998;Srinivasan et al 2005), roe 1 (Ma et al 1996) (synonym da 10 , gift from Claire Cronmiller) (Brown et al 1996), da 1 (Bell 1954), eya 2 (Bonini et al 1993), Star 1 (Lewis 1945;Higson et al 1993), Dl RevF10 Ser RX82 P{neoFRT}82B (Zeng et al 1998), osa 308 P{neoFRT}82B (Treisman et al 1997;Janody et al 2004), trx E2 P{neoFRT}82B ( Janody et al 2004), brm T485 P{neoFRT}80B ( Janody et al 2004), and snr1…”

Section: Methodsmentioning

confidence: 99%

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Identification of Novel Regulators of atonal Expression in the Developing Drosophila Retina

et al. 2008

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Atonal is a Drosophila proneural protein required for the proper formation of the R8 photoreceptor cell, the founding photoreceptor cell in the developing retina. Proper expression and refinement of the Atonal protein is essential for the proper formation of the Drosophila adult eye. In vertebrates, expression of transcription factors orthologous to Drosophila Atonal (MATH5/Atoh7, XATH5, and ATH5) and their progressive restriction are also involved in specifying the retinal ganglion cell, the founding neural cell type in the mammalian retina. Thus, identifying factors that are involved in regulating the expression of Atonal during development are important to fully understand how retinal neurogenesis is accomplished. We have performed a chemical mutagenesis screen for autosomal dominant enhancers of a loss-offunction atonal eye phenotype. We report here the identification of five genes required for proper Atonal expression, three of which are novel regulators of Atonal expression in the Drosophila retina. We characterize the role of the daughterless, kismet, and roughened eye genes on atonal transcriptional regulation in the developing retina and show that each gene regulates atonal transcription differently within the context of retinal development. Our results provide additional insights into the regulation of Atonal expression in the developing Drosophila retina.

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Section: Ao9mentioning

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Identification of Novel Regulators of atonal Expression in the Developing Drosophila Retina

et al. 2008

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“…To date, the Consensus Coding Sequence (CCDS) database has reported that ARID1B encodes a large isoform of 2,249 amino acids (CCDS55072.1) and a smaller isoform of 2,236 amino acids (CCDS5251.2). The first functional studies of Arid1b analyzed the Drosophila protein (initially termed eyelid and subsequently renamed Osa), which was found to be important in embryonic segmentation, development of the notum and wing margin, and photoreceptor differentiation in flies (19). Subsequent studies using genetic and biochemical approaches indicated that the protein binds to DNA without sequence specificity and that the protein is a subunit of BAF complexes containing a core ATP-dependent helicase called Brahma (BRM) (20,21).…”

Section: What Is Arid1b?mentioning

confidence: 99%

ARID1B-mediated disorders: Mutations and possible mechanisms

Sim

White

Lockhart

2015

IRDR

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“…The p250 protein shows strong sequence homology to the Drosophila Osa/eyelid protein. Osa/eyelid, originally identified as a trithorax group member (69), has organ-specific genetic interactions with brm, mor, and snr1 (homologs of SNF2/SWI2, SWI3, and SNF5, respectively) and antagonizes wingless signaling (70,71). Both of the p250 and p250R proteins have a highly conserved region, referred to as the ARID domain (72), that has been found in more than a dozen other proteins (Fig.…”

Section: Syt Protein Is Present In Native Snf/swi Complexes-mentioning

confidence: 99%

SYT Associates with Human SNF/SWI Complexes and the C-terminal Region of Its Fusion Partner SSX1 Targets Histones

Kato¹,

Tjernberg²,

Zhang³

et al. 2002

Journal of Biological Chemistry

101

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A global transcriptional co-activator, the SNF/SWI complex, has been characterized as a chromatin remodeling factor that enhances accessibility of the transcriptional machinery to DNA within a repressive chromatin structure. On the other hand, mutations in some human SNF/SWI complex components have been linked to tumor formation. We show here that SYT, a partner protein generating the synovial sarcoma fusion protein SYT-SSX, associates with native human SNF/SWI complexes. The SYT protein has a unique QPGY domain, which is also present in the largest subunits, p250 and the newly identified homolog p250R, of the corresponding SNF/SWI complexes. The C-terminal region (amino acids 310 -387) of SSX1, comprising the SSX1 portion of the SYT-SSX1 fusion protein, binds strongly to core histones and oligonucleosomes in vitro and directs nuclear localization of a green fluorescence protein fusion protein. Experiments with serial C-terminal deletion mutants of SSX1 indicate that these properties map to a common region and also correlate with the previously demonstrated anchorage-independent colony formation activity of SYT-SSX in Rat 3Y1 cells. These data suggest that SYT-SSX interferes with the function of either the SNF/SWI complexes or another SYT-interacting co-activator, p300, by changing their targeted localization or by directly inhibiting their chromatin remodeling activities.The chromatin structure of active eukaryotic genes is subject to dynamic change by chromatin modifiers such as ATP-dependent chromatin remodeling factors (reviewed in Refs. 1-5). Homologs of a yeast prototype ATP-dependent remodeling complex, SNF/SWI, appear to be widely present in eukaryotes from yeast to humans (6 -8). Functions of the subunits of the SNF/ SWI complexes (9, 10) were first demonstrated by genetic studies in Saccharomyces cerevisiae, which showed that SWI1/ ADR6, SWI2/SNF2, SWI3, and SNF5 are required for the expression of a set of genes that include the HO, GAL1, SUC2, and ADH2 genes (11-13). In Drosophila melanogaster, the SWI2/SNF2 homolog brm was originally identified as a suppressor of Polycomb mutations (14). The Drosophila complex has been isolated, and some of the subunits have been characterized (15, 16), revealing that the SNF/SWI complexes are highly conserved in subunit composition and in primary structure among yeast, fruit fly, and human. A number of studies have described various biochemical properties of the human and yeast SNF/SWI complexes, as well as other ATP-dependent chromatin remodeling complexes (reviewed in Refs. 1-3, 17). For instance the SNF/SWI complexes are recruited by transcriptional activators to nucleosomal templates (18 -23), perturb nucleosome positioning, and facilitate binding of activator proteins to nucleosomes (24 -26). Mechanisms for this perturbation have been proposed to involve interconversion between two different nucleosomal states (27), sliding of histone octamers (28) or a change of DNA topology (29, 30).The human complexes are composed of at least nine subunits that include appar...

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eyelidantagonizes wingless signaling during Drosophiladevelopment and has homology to the Bright family of DNA-binding proteins

Cited by 98 publications

References 108 publications

Identification of Novel Regulators of atonal Expression in the Developing Drosophila Retina

Identification of Novel Regulators of atonal Expression in the Developing Drosophila Retina

<i>ARID1B</i>-mediated disorders: Mutations and possible mechanisms

SYT Associates with Human SNF/SWI Complexes and the C-terminal Region of Its Fusion Partner SSX1 Targets Histones

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