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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

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
Authors
Issue Date2000
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/leu
Citation
Leukemia, 2000, v. 14 n. 1, p. 77-83 How to Cite?
Abstract
Retinoic 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.
Persistent Identifierhttp://hdl.handle.net/10722/148192
ISSN
2013 Impact Factor: 9.379
2013 SCImago Journal Rankings: 4.500
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSo, CWen_US
dc.contributor.authorDong, Sen_US
dc.contributor.authorSo, CKCen_US
dc.contributor.authorCheng, GXen_US
dc.contributor.authorHuang, QHen_US
dc.contributor.authorChen, SJen_US
dc.contributor.authorChan, LCen_US
dc.date.accessioned2012-05-29T06:11:23Z-
dc.date.available2012-05-29T06:11:23Z-
dc.date.issued2000en_US
dc.identifier.citationLeukemia, 2000, v. 14 n. 1, p. 77-83en_US
dc.identifier.issn0887-6924en_US
dc.identifier.urihttp://hdl.handle.net/10722/148192-
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.en_US
dc.languageengen_US
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/leuen_US
dc.relation.ispartofLeukemiaen_US
dc.subject.meshDimerizationen_US
dc.subject.meshHumansen_US
dc.subject.meshLeukemia, Promyelocytic, Acute - Drug Therapy - Metabolismen_US
dc.subject.meshNeoplasm Proteins - Metabolismen_US
dc.subject.meshOncogene Proteins, Fusion - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshTrans-Activators - Metabolismen_US
dc.subject.meshTretinoin - Therapeutic Useen_US
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 leukemiaen_US
dc.typeArticleen_US
dc.identifier.emailChan, LC:chanlc@hkucc.hku.hken_US
dc.identifier.authorityChan, LC=rp00373en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid10637480en_US
dc.identifier.scopuseid_2-s2.0-0033964844en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033964844&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume14en_US
dc.identifier.issue1en_US
dc.identifier.spage77en_US
dc.identifier.epage83en_US
dc.identifier.isiWOS:000084925300011-
dc.publisher.placeUnited Kingdomen_US

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