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Article: The impact of differential binding of wild-type RARA, PML-, PLZF- and NPM-RARA fusion proteins towards transcriptional co-activator, RIP-140, on retinoic acid responses in acute promyelocytic leukemia
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TitleThe impact of differential binding of wild-type RARA, PML-, PLZF- and NPM-RARA fusion proteins towards transcriptional co-activator, RIP-140, on retinoic acid responses in acute promyelocytic leukemia
 
AuthorsSo, CW1
Dong, S2
So, CKC1
Cheng, GX2
Huang, QH3
Chen, SJ3
Chan, LC1
 
Issue Date2000
 
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/leu
 
CitationLeukemia, 2000, v. 14 n. 1, p. 77-83 [How to Cite?]
 
AbstractRetinoic acid receptor (RA) heterodimer (RAR/RXR) activities have been shown to be repressed by transcriptional co-repressor, SMRT/N-CoR, in the absence of the ligand while upon all-trans retionic acid (ATRA) treatment, SMRT/N-CoR is dissociated from RARA(U leading to gene expression by the recruitment of transcriptional co-activators to the transcriptional complex. The difference in response to ATRA therapy between acute promyelocytic leukemia (APL) patients with PML-RARA(U fusion and PLZF-RARA fusion has recently been found to be partially due to the strong association of the transcriptional co-repressor, SMRT/N-CoR, with PLZF domain. We demonstrate that SMRT association, as with PML-RARA, can be released from NPM-RARA at pharmacological concentration of ATRA (10 -6 M). Moreover, we show for the first time that the interaction between the transcriptional co-activator, RIP-140, and PML-, PLZF- or NPM-RARA fusion proteins can be positively stimulated by ATRA although they are less sensitive as compared with the wild-type RARA. Our results suggest that the dissociation of transcriptional co-repressors, SMRT/N-CoR, and recruitment of co-activators, eg RIP-140, to APL-associated fusion proteins constitute a common molecular mechanism in APL and underlie the responsiveness of the disease to RA therapy.
 
ISSN0887-6924
2013 Impact Factor: 9.379
2013 SCImago Journal Rankings: 4.500
 
ISI Accession Number IDWOS:000084925300011
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorSo, CW
 
dc.contributor.authorDong, S
 
dc.contributor.authorSo, CKC
 
dc.contributor.authorCheng, GX
 
dc.contributor.authorHuang, QH
 
dc.contributor.authorChen, SJ
 
dc.contributor.authorChan, LC
 
dc.date.accessioned2012-05-29T06:11:23Z
 
dc.date.available2012-05-29T06:11:23Z
 
dc.date.issued2000
 
dc.description.abstractRetinoic acid receptor (RA) heterodimer (RAR/RXR) activities have been shown to be repressed by transcriptional co-repressor, SMRT/N-CoR, in the absence of the ligand while upon all-trans retionic acid (ATRA) treatment, SMRT/N-CoR is dissociated from RARA(U leading to gene expression by the recruitment of transcriptional co-activators to the transcriptional complex. The difference in response to ATRA therapy between acute promyelocytic leukemia (APL) patients with PML-RARA(U fusion and PLZF-RARA fusion has recently been found to be partially due to the strong association of the transcriptional co-repressor, SMRT/N-CoR, with PLZF domain. We demonstrate that SMRT association, as with PML-RARA, can be released from NPM-RARA at pharmacological concentration of ATRA (10 -6 M). Moreover, we show for the first time that the interaction between the transcriptional co-activator, RIP-140, and PML-, PLZF- or NPM-RARA fusion proteins can be positively stimulated by ATRA although they are less sensitive as compared with the wild-type RARA. Our results suggest that the dissociation of transcriptional co-repressors, SMRT/N-CoR, and recruitment of co-activators, eg RIP-140, to APL-associated fusion proteins constitute a common molecular mechanism in APL and underlie the responsiveness of the disease to RA therapy.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationLeukemia, 2000, v. 14 n. 1, p. 77-83 [How to Cite?]
 
dc.identifier.epage83
 
dc.identifier.isiWOS:000084925300011
 
dc.identifier.issn0887-6924
2013 Impact Factor: 9.379
2013 SCImago Journal Rankings: 4.500
 
dc.identifier.issue1
 
dc.identifier.pmid10637480
 
dc.identifier.scopuseid_2-s2.0-0033964844
 
dc.identifier.spage77
 
dc.identifier.urihttp://hdl.handle.net/10722/148192
 
dc.identifier.volume14
 
dc.languageeng
 
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/leu
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofLeukemia
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshDimerization
 
dc.subject.meshHumans
 
dc.subject.meshLeukemia, Promyelocytic, Acute - Drug Therapy - Metabolism
 
dc.subject.meshNeoplasm Proteins - Metabolism
 
dc.subject.meshOncogene Proteins, Fusion - Metabolism
 
dc.subject.meshProtein Binding
 
dc.subject.meshTrans-Activators - Metabolism
 
dc.subject.meshTretinoin - Therapeutic Use
 
dc.titleThe impact of differential binding of wild-type RARA, PML-, PLZF- and NPM-RARA fusion proteins towards transcriptional co-activator, RIP-140, on retinoic acid responses in acute promyelocytic leukemia
 
dc.typeArticle
 
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<contributor.author>Chen, SJ</contributor.author>
<contributor.author>Chan, LC</contributor.author>
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Author Affiliations
  1. The University of Hong Kong
  2. Shanghai Transgenic Research Center
  3. Shanghai Second Medical University