Nuclear Receptor Coactivator ACTR Is a Novel Histone Acetyltransferase and Forms a Multimeric Activation Complex with P/CAF and CBP/p300

Chen, Hongwu; Lin, Richard J.; Schiltz, R. Louis; Chakravarti, Debabrata; Nash, Alyssa; Nagy, László; Privalsky, Martin L.; Nakatani, Yoshihiro; Evans, Ronald M.

doi:10.1016/s0092-8674(00)80516-4

Cited by 1,377 publications

(1,060 citation statements)

References 55 publications

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“…Note in this respect that PLZF was shown to speci®cally bind the N-Cor and SMRT co-repressors (Dhordain et al, 1997;Hong et al, 1997). These proteins recruit histone deacetylase complexes and could induce irreversible changes in the chromatin state (Chen et al, 1997b;Nagy et al, 1997;Grignani et al, 1998;Guidez et al, 1998;Lin et al, 1998). The third explanation is an implication of the reciprocal RARa/PLZF product, whose mRNA is found in all t(11;17) patients.…”

Section: Discussionmentioning

confidence: 98%

Retinoic acid, but not arsenic trioxide, degrades the PLZF/RARα fusion protein, without inducing terminal differentiation or apoptosis, in a RA-therapy resistant t(11;17)(q23;q21) APL patient

Koken

Daniel²,

Giannı̀

et al. 1999

Oncogene

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Primary blasts of a t(11;17)(q23;q21) acute promyelocytic leukaemia (APL) patient were analysed with respect to retinoic acid (RA) and arsenic trioxide (As 2 O 3 ) sensitivity as well as PLZF/RARa status. Although RA induced partial monocytic di erentiation ex vivo, but not in vivo, As203 failed to induce apoptosis in culture, contrasting with t(15;17) APL and arguing against the clinical use of As203 in t(11;17)(q23;q21) APL. Prior to cell culture, PLZF/RARa was found to exactly co-localize with PML onto PML nuclear bodies. However upon cell culture, it quickly shifted towards microspeckles, its localization found in transfection experiments. Arsenic trioxide, known to induce aggregation of PML nuclear bodies, left the microspeckled PLZF/RARa localization completely una ected. RA treatment led to PLZF/RARa degradation. However, this complete PLZF/RARa degradation was not accompanied by di erentiation or apoptosis, which could suggest a contribution of the reciprocal RARa/PLZF fusion product in leukaemogenesis or the existence of irreversible changes induced by the chimera.

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Section: Discussionmentioning

confidence: 98%

Retinoic acid, but not arsenic trioxide, degrades the PLZF/RARα fusion protein, without inducing terminal differentiation or apoptosis, in a RA-therapy resistant t(11;17)(q23;q21) APL patient

Koken

Daniel²,

Giannı̀

et al. 1999

Oncogene

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“…A recent clinical study using 560 human breast tumor tissues found the AIB1 expression along with expression of genes involved in cell migration and invasion such as polyomavirus enhancer activator 3 and matrix metalloproteinases 2 and 9 suggesting a positive correlation of AIB1 expression with tumor metastasis [95]. The AIB1 coactivator activates ERα-dependent transcription by recruiting HAT such as p300 and P/CAF to ERα target gene chromatin [175]. AIB1 interacts with ERα in a ligand-dependent fashion and its coactivator activity is potentiated by CK1δ and PKCε-mediated phosphorylation of AIB1 in breast cancer cells [176,177].…”

Section: Estrogen Receptor Coregulators In Breast Cancer Coactivatorsmentioning

confidence: 99%

RETRACTED ARTICLE: Regulation of estrogen receptor signaling in breast carcinogenesis and breast cancer therapy

Zhou

Qiao

Shetty

et al. 2013

Cell. Mol. Life Sci.

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Estrogen and estrogen receptors (ERs) are critical regulators of breast epithelial cell proliferation, differentiation, and apoptosis. Compromised signaling vis-à-vis the estrogen receptor is believed © Springer Basel 2013 yow4@pitt.edu. ), which predicts for response to endocrine-based therapy; however, innate or acquired resistance to endocrinebased drugs remains a serious challenge. The complexity of regulation for estrogen signaling coupled with the crosstalk of other oncogenic signaling pathways is a reason for endocrine therapy resistance. Alternative strategies that target novel molecular mechanisms are necessary to overcome this current and urgent gap in therapy. A thorough analysis of estrogen-signaling regulation is critical. In this review article, we will summarize current insights into the regulation of estrogen signaling as related to breast carcinogenesis and breast cancer therapy. NIH Public Access

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“…Transcriptional squelching between members of the nuclear receptor family suggested the existence of intermediary cofactors. A number of nuclear receptor interacting proteins have been characterized that speci®cally bind to the hormone-binding domain of the receptor in the presence of ligand, some of them, including histone acetyltransferases like CBP and its homolog p300, P/ CAF and ACTR were shown to behave unequivocally as true co-activators (Chen et al (1997) and references therein). Conversely, in the absence of ligand, RARs (and their related thyroid hormone receptors TRs) behave as transcriptional repressors.…”

Section: Introductionmentioning

confidence: 99%

Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein

et al. 1998

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The PLZF gene was identi®ed ®rst by its fusion with the retinoic acid receptor a gene in the t(11;17) translocation associated with a retinoic acid resistant form of acute promyelocytic leukemia (APL). It encodes a kruÈppel-like zinc ®nger protein with a POZ domain shared with a subset of regulatory proteins including the BCL6 leukemogenic protein. PLZF, like BCL6, strongly represses transcription initiated from di erent promoters. Here we show that PLZF associates in vitro and in vivo with the Mad co-repressor mSin3A and the histone deacetylase HDAC1. Two domains in PLZF and the PAH1 structure of mSin3A mediate these interactions. Trichostatin A, a speci®c inhibitor of histone deacetylases, signi®cantly reduces PLZF repression. These data strongly suggest that, like nuclear receptors and Mad, PLZF represses transcription by recruiting a histone deacetylase through the SMRT-mSin3-HDAC co-repressor complex. We also show that BCL6 associates with HDAC1 indicating that this type of regulation might be common to POZ/Zinc ®nger proteins involved in human leukemias. This work supports a role for deregulated histone deacetylation in the development of both lymphoid and myeloid neoplasia in human and suggests that targeted histone deacetylase inhibitors may be useful for treatment of certain types of malignancies.

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Nuclear Receptor Coactivator ACTR Is a Novel Histone Acetyltransferase and Forms a Multimeric Activation Complex with P/CAF and CBP/p300

Cited by 1,377 publications

References 55 publications

Retinoic acid, but not arsenic trioxide, degrades the PLZF/RARα fusion protein, without inducing terminal differentiation or apoptosis, in a RA-therapy resistant t(11;17)(q23;q21) APL patient

Retinoic acid, but not arsenic trioxide, degrades the PLZF/RARα fusion protein, without inducing terminal differentiation or apoptosis, in a RA-therapy resistant t(11;17)(q23;q21) APL patient

RETRACTED ARTICLE: Regulation of estrogen receptor signaling in breast carcinogenesis and breast cancer therapy

Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein

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