RETRACTED: Nuclear Receptor Function Requires a TFTC-Type Histone Acetyl Transferase Complex

Yanagisawa, Junn; Kitagawa, Hirochika; Yanagida, Mitsuaki; Wada, Osamu; Ogawa, Shinpei; Nakagomi, Madoka; Oishi, Hajime; Yamamoto, Yasuhiko; Nagasawa, Hiromich; McMahon, Steven B.; Cole, Michael; Tora, Làszlò; Takahashi, Nobuhiro; Kato, Shigeaki

doi:10.1016/s1097-2765(02)00478-1

Cited by 147 publications

(150 citation statements)

References 44 publications

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“…The protein composition of these complexes determines the overall transcriptional effect exerted by the receptor (Yanagisawa et al, 2002;Kitagawa et al, 2003;Ohtake et al, 2003). Interaction of retinoid receptors with b-catenin at the Id2 gene WRE presumably leads to recruitment of repressor complexes containing histone deacetylase and demethylase activities.…”

Section: Discussionmentioning

confidence: 99%

Id2 gene-targeted crosstalk between Wnt and retinoid signaling regulates proliferation in human keratinocytes

et al. 2007

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We investigated the effect of all-trans-retinoic acid (atRA) on proliferation in several human skin cell lines and found that antiproliferative potency of atRA correlated with the endogenous activity of canonical Wnt signaling. In HaCaT keratinocytes, we found that atRA significantly suppressed the expression of Id2, a member of the inhibitor of differentiation family of transcription factors that regulate cell growth and differentiation. However, no apparent change in the expression of other Wnt targets, like c-Myc or cyclin D1, was observed. Retinoid-induced Id2 gene suppression was associated with decreased levels of histone H3 and H4 acetylation and histone H3 Lys-4 methylation, and with recruitment of the LSD1 demethylase at the Wnt-response element (WRE) (TCF/LEF-binding site), in the Id2 gene promoter. None of such changes was detected at the WRE of c-Myc and cyclin D1 gene promoters. Inhibition of Id2 by short interfering RNA (siRNA) had a similar effect on the proliferation of HaCaT cells as exposure to atRA, whereas anti-b-catenin siRNA significantly inhibited its antiproliferative effect. These data suggest that downregulation of Id2 gene expression through transcriptional convergence between Wnt and retinoid signaling pathways underlies the antiproliferative effect of retinoids in keratinocytes, and provide evidence of gene-targeted crosstalk between signaling pathways.

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Section: Discussionmentioning

confidence: 99%

Id2 gene-targeted crosstalk between Wnt and retinoid signaling regulates proliferation in human keratinocytes

et al. 2007

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“…These include c-Myc, p53, E2F1, E2F4, E1A, ERa, ERb, VDR, PPARg, LXR, FXR, b-catenin, Skp1 and BRCA1 Lang et al, 2001;Park et al, 2001;Ard et al, 2002;Yanagisawa et al, 2002;Lang and Hearing, 2003;Unno et al, 2005;Cheng et al, 2006;Oishi et al, 2006;Sierra et al, 2006;Finkbeiner and Herceg, unpublished results). Interestingly, the TRRAP domains that interact with diverse partners are not overlapping and it can be speculated that TRRAP may serve not only as a scaffold for HAT complexes but also as a platform for recruitment of different regulatory factors and complexes to chromatin.…”

Section: Cellular Pools Of Trrapmentioning

confidence: 91%

“…The TRRAP (TRansformation/tRanscription domainAssociated Protein) and its yeast homolog Tra1, remarkably large proteins with homology to the phosphatidyl-inositol-3-kinase (PI3K) family members are common components of many HAT complexes in yeast and mammalian cells (Grant et al, 1998;Vassilev et al, 1998;Allard et al, 1999;Brand et al, 1999;Ikura et al, 2000;Pray-Grant et al, 2002;Sterner et al, 2002). TRRAP was originally identified in the Michael Cole's laboratory as an interacting partner of c-Myc , and subsequent studies showed that several other transcription factors including E2F and nuclear receptors interact with TRRAP Lang et al, 2001;Yanagisawa et al, 2002;Fan et al, 2004). Interestingly, TRRAP/Tra1 appears to be the only component through which HAT complexes (either histone H3 acetylating complexes or those with preference for histone H4) contact transcription activators (Brown et al, 2001;Bhaumik et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Orchestration of chromatin-based processes: mind the TRRAP

et al. 2007

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Chromatin modifications at core histones including acetylation, methylation, phosphorylation and ubiquitination play an important role in diverse biological processes. Acetylation of specific lysine residues within the N terminus tails of core histones is arguably the most studied histone modification; however, its precise roles in different cellular processes and how it is disrupted in human diseases remain poorly understood. In the last decade, a number of histone acetyltransferases (HATs) enzymes responsible for histone acetylation, has been identified and functional studies have begun to unravel their biological functions. The activity of many HATs is dependent on HAT complexes, the multiprotein assemblies that contain one HAT catalytic subunit, adapter proteins, several other molecules of unknown function and a large protein called TRansformation/tRanscription domain-Associated Protein (TRRAP). As a common component of many HAT complexes, TRRAP appears to be responsible for the recruitment of these complexes to chromatin during transcription, replication and DNA repair. Recent studies have shed new light on the role of TRRAP in HAT complexes as well as mechanisms by which it mediates diverse cellular processes. Thus, TRRAP appears to be responsible for a concerted and context-dependent recruitment of HATs and coordination of distinct chromatin-based processes, suggesting that its deregulation may contribute to diseases. In this review, we summarize recent developments in our understanding of the function of TRRAP and TRRAP-containing HAT complexes in normal cellular processes and speculate on the mechanism underlying abnormal events that may lead to human diseases such as cancer.

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“…GST-fused proteins were expressed in E. coli and purified on glutathione-Sepharose beads (Amersham Pharmacia). Pull-down assays were performed as described (10,16,(19)(20)(21). Immobilized glutathione-Sepharose and avidin-resin were incubated with 35 S-methionine-labeled SF3a p120 protein.…”

Section: Methodsmentioning

confidence: 99%

“…The best-characterized complex contains p160͞SRC family proteins (3,4) and CBP͞p300 histone acetyltransferases (5,6), along with the RNA coactivator steroid receptor RNA activator (7) and presumably other known and unknown coactivators (8,9). Another histone acetyltransferasescontaining complex, the TBP-free TAF II -containing (TFTC)-like complex (10), can also coactivate ER transactivation, as can the nonhistone acetyltransferases DRIP (VDR interacting protein)͞TRAP (thyroid hormone receptor-associated protein)͞ SMCC (SRB͞MED cofactor complexes)͞ARC (activatorrecruited cofactor) complex (11)(12)(13).…”

mentioning

confidence: 99%

Splicing potentiation by growth factor signals via estrogen receptor phosphorylation

Masuhiro

Mezaki²,

Sakari³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Mitogen-activated protein kinase-mediated growth factor signals are known to augment the ligand-induced transactivation function of nuclear estrogen receptor ␣ (ER␣) through phosphorylation of Ser-118 within the ER␣ N-terminal transactivation (activation function-1) domain. We identified the spliceosome component splicing factor (SF)3a p120 as a coactivator specific for human ER␣ (hER␣) activation function-1 that physically associated with ER␣ dependent on the phosphorylation state of Ser-118. SF3a p120 potentiated hER␣-mediated RNA splicing, and notably, the potentiation of RNA splicing by SF3a p120 depended on hER Ser-118 phosphorylation. Thus, our findings suggest a mechanism by which growth factor signaling can regulate gene expression through the modulation of RNA splicing efficiency via phosphorylation of sequencespecific activators, after association between such activators and the spliceosome.nuclear receptor ͉ estrogen ͉ coactivator ͉ mitogen-activated protein kinase ͉ RNA splicing M ost of the actions of estrogen are thought to be mediated via the transcriptional control of target genes by nuclear estrogen receptors (ER) ␣ and ␤, members of the steroid hormone receptor gene superfamily that act as ligand-inducible transcription factors. ERs bind as dimers to specific estrogen response elements in the promoters of some target genes (1). However, most ER target promoters appear to recruit ERs without specific DNA binding, presumably through associations with sequence-specific factors bound to the promoters (2). ERs contain two transactivation functions (AFs), AF-1 in the Nterminal A͞B domain and AF-2 in the C-terminal ligand-binding E͞F domain. Ligand-induced transactivation by ERs requires multiple distinct classes of coactivator complexes, as well as a number of coregulators. The best-characterized complex contains p160͞SRC family proteins (3, 4) and CBP͞p300 histone acetyltransferases (5, 6), along with the RNA coactivator steroid receptor RNA activator (7) and presumably other known and unknown coactivators (8, 9). Another histone acetyltransferasescontaining complex, the TBP-free TAF II -containing (TFTC)-like complex (10), can also coactivate ER transactivation, as can the nonhistone acetyltransferases DRIP (VDR interacting protein)͞TRAP (thyroid hormone receptor-associated protein)͞ SMCC (SRB͞MED cofactor complexes)͞ARC (activatorrecruited cofactor) complex (11-13).ER-mediated estrogen signaling is known to involve cross-talk with other signaling pathways (14). For instance, growth factors potentiate estrogen-induced cellular proliferation in female reproductive tissues (15). Phosphorylation of the Ser-118 residue in the human ER␣ (hER␣) A͞B domain by mitogen-activated protein kinase (MAPK) activated by growth factors (16, 17) and cyclin-dependent kinase-7 (18) results in the potentiation of AF-1 function (16). However, the molecular basis of ER␣ AF-1 potentiation by MAPK-mediated phosphorylation remains unclear. In a previous study, we identified the DEAD-box RNA helicase subfamily member p68͞p72...

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RETRACTED: Nuclear Receptor Function Requires a TFTC-Type Histone Acetyl Transferase Complex

Cited by 147 publications

References 44 publications

Id2 gene-targeted crosstalk between Wnt and retinoid signaling regulates proliferation in human keratinocytes

Id2 gene-targeted crosstalk between Wnt and retinoid signaling regulates proliferation in human keratinocytes

Orchestration of chromatin-based processes: mind the TRRAP

Splicing potentiation by growth factor signals via estrogen receptor phosphorylation

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