Differential roles of PML isoforms
The tumor suppressor promyelocytic leukemia protein (PML) is fused to the retinoic acid receptor alpha in patients suffering from acute promyelocytic leukemia (APL). Treatment of APL patients with arsenic trioxide (As2O3) reverses the disease phenotype by a process involving the degradation of the f...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Frontiers Media S.A.
2013-05-01
|
Series: | Frontiers in Oncology |
Subjects: | |
Online Access: | http://journal.frontiersin.org/Journal/10.3389/fonc.2013.00125/full |
_version_ | 1818303083297374208 |
---|---|
author | Sébastien eNisole Sébastien eNisole Mohamed Ali eMaroui Mohamed Ali eMaroui Xavier eMascle Muriel eAubry Mounira K Chelbi-Alix Mounira K Chelbi-Alix |
author_facet | Sébastien eNisole Sébastien eNisole Mohamed Ali eMaroui Mohamed Ali eMaroui Xavier eMascle Muriel eAubry Mounira K Chelbi-Alix Mounira K Chelbi-Alix |
author_sort | Sébastien eNisole |
collection | DOAJ |
description | The tumor suppressor promyelocytic leukemia protein (PML) is fused to the retinoic acid receptor alpha in patients suffering from acute promyelocytic leukemia (APL). Treatment of APL patients with arsenic trioxide (As2O3) reverses the disease phenotype by a process involving the degradation of the fusion protein via its PML moiety. Several PML isoforms are generated from a single PML gene by alternative splicing. They share the same N-terminal region containing the RBCC/TRIM motif but differ in their C-terminal sequences. Recent studies of all the PML isoforms reveal the specific functions of each. Here, we review the nomenclature and structural organization of the PML isoforms in order to clarify the various designations and classifications found in different databases. The functions of the PML isoforms and their differential roles in antiviral defense also are reviewed. Finally, the key players involved in the degradation of the PML isoforms in response to As2O3 or other inducers are discussed. |
first_indexed | 2024-12-13T05:49:09Z |
format | Article |
id | doaj.art-e60ed5abc7bf4ecea9578a50435858ac |
institution | Directory Open Access Journal |
issn | 2234-943X |
language | English |
last_indexed | 2024-12-13T05:49:09Z |
publishDate | 2013-05-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Oncology |
spelling | doaj.art-e60ed5abc7bf4ecea9578a50435858ac2022-12-21T23:57:36ZengFrontiers Media S.A.Frontiers in Oncology2234-943X2013-05-01310.3389/fonc.2013.0012551002Differential roles of PML isoformsSébastien eNisole0Sébastien eNisole1Mohamed Ali eMaroui2Mohamed Ali eMaroui3Xavier eMascle4Muriel eAubry5Mounira K Chelbi-Alix6Mounira K Chelbi-Alix7INSERM UMR-S 747Université Paris DescartesCNRS FRE3235Université Paris DescartesUniversité de MontréalUniversité de MontréalCNRS FRE3235Université Paris DescartesThe tumor suppressor promyelocytic leukemia protein (PML) is fused to the retinoic acid receptor alpha in patients suffering from acute promyelocytic leukemia (APL). Treatment of APL patients with arsenic trioxide (As2O3) reverses the disease phenotype by a process involving the degradation of the fusion protein via its PML moiety. Several PML isoforms are generated from a single PML gene by alternative splicing. They share the same N-terminal region containing the RBCC/TRIM motif but differ in their C-terminal sequences. Recent studies of all the PML isoforms reveal the specific functions of each. Here, we review the nomenclature and structural organization of the PML isoforms in order to clarify the various designations and classifications found in different databases. The functions of the PML isoforms and their differential roles in antiviral defense also are reviewed. Finally, the key players involved in the degradation of the PML isoforms in response to As2O3 or other inducers are discussed.http://journal.frontiersin.org/Journal/10.3389/fonc.2013.00125/fullvirusSUMORNF4CK2TRIMPML isoforms |
spellingShingle | Sébastien eNisole Sébastien eNisole Mohamed Ali eMaroui Mohamed Ali eMaroui Xavier eMascle Muriel eAubry Mounira K Chelbi-Alix Mounira K Chelbi-Alix Differential roles of PML isoforms Frontiers in Oncology virus SUMO RNF4 CK2 TRIM PML isoforms |
title | Differential roles of PML isoforms |
title_full | Differential roles of PML isoforms |
title_fullStr | Differential roles of PML isoforms |
title_full_unstemmed | Differential roles of PML isoforms |
title_short | Differential roles of PML isoforms |
title_sort | differential roles of pml isoforms |
topic | virus SUMO RNF4 CK2 TRIM PML isoforms |
url | http://journal.frontiersin.org/Journal/10.3389/fonc.2013.00125/full |
work_keys_str_mv | AT sebastienenisole differentialrolesofpmlisoforms AT sebastienenisole differentialrolesofpmlisoforms AT mohamedaliemaroui differentialrolesofpmlisoforms AT mohamedaliemaroui differentialrolesofpmlisoforms AT xavieremascle differentialrolesofpmlisoforms AT murieleaubry differentialrolesofpmlisoforms AT mounirakchelbialix differentialrolesofpmlisoforms AT mounirakchelbialix differentialrolesofpmlisoforms |