Reference Report

Reference
Citation	Wang, L., Charroux, B., Kerridge, S., Tsai, C.C. (2008). Atrophin recruits HDAC1/2 and G9a to modify histone H3K9 and to determine cell fates. EMBO Rep. 9(6): 555--562. (Export to RIS)
FlyBase ID	FBrf0205145
Publication Type	Research paper
PubMed ID	18451879
PubMed Abstract	Atrophin family proteins, including the vertebrate arginine-glutamic acid dipeptide repeats protein (RERE) and Drosophila Atrophin (Atro), constitute a new class of nuclear receptor corepressors. Both RERE and Atro share the ELM2 (EGL-27 and MTA1 homology 2) and SANT (SWI3/ADA2/N-CoR/TFIII-B) domains, which are also present in other important transcriptional cofactors. Here, we report that the SANT domain in RERE binds to the histone methyltransferase G9a, and that both the ELM2 and SANT domains orchestrate molecular events that lead to a stable methylation of histone H3-lysine 9. We establish the physiological relevance of these interactions among Atrophin, G9a, and histone deacetylases 1 and 2 in Drosophila by showing that these proteins localize to overlapping chromosomal loci, and act together to suppress wing vein and melanotic-mass formation. This study not only shows a new function of the SANT domain and establishes its connection with the ELM2 domain, but also implies that a similar strategy is used by other ELM2-SANT proteins to repress gene transcription and to exert biological effects.
DOI	10.1038/embor.2008.67
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Language of Publication	English
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Publication Type	Journal
Abbreviation	EMBO Rep.
Title	EMBO Reports
Publication Year	2000-
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Data from Reference
Alleles (15)
	Avic\GFP^Scer\UAS.cUa Disc\RFP^{DsRedT4.Scer\UAS.T:nls-tra} Egfr^E1 Egfr^t1 G9a^del34 G9a^RG5 Gug³⁵ Gug^{dsRNA.1.Scer\UAS} Gug^{dsRNA.2.Scer\UAS} Gug^Scer\UAS.cCa Rpd3³¹³ Rpd3⁰⁴⁵⁵⁶ Scer\GAL4^dpp.blk1 Scer\GAL4^ey.PH Scer\GAL4^hs.PB
Constructs (8)
	P{GAL4-dpp.blk1} P{GAL4-ey.H} P{GAL4-Hsp70.PB} P{UAS-Atro.C} P{UAS-GFP.U} P{UAS-Gug.IR1} P{UAS-Gug.IR2} P{UAS-RedStinger}
Genes (8)
	Avic\GFP Disc\RFP Egfr G9a Gug His3 Rpd3 Scer\GAL4