Cargando…
PIAS1 interacts with FLASH and enhances its co-activation of c-Myb
BACKGROUND: FLASH is a huge nuclear protein involved in various cellular functions such as apoptosis signalling, NF-κB activation, S-phase regulation, processing of histone pre-mRNAs, and co-regulation of transcription. Recently, we identified FLASH as a co-activator of the transcription factor c-My...
Autores principales: | , , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3050860/ https://www.ncbi.nlm.nih.gov/pubmed/21338522 http://dx.doi.org/10.1186/1476-4598-10-21 |
_version_ | 1782199408627023872 |
---|---|
author | Alm-Kristiansen, Anne Hege Lorenzo, Petra I Molværsmyr, Ann-Kristin Matre, Vilborg Ledsaak, Marit Sæther, Thomas Gabrielsen, Odd S |
author_facet | Alm-Kristiansen, Anne Hege Lorenzo, Petra I Molværsmyr, Ann-Kristin Matre, Vilborg Ledsaak, Marit Sæther, Thomas Gabrielsen, Odd S |
author_sort | Alm-Kristiansen, Anne Hege |
collection | PubMed |
description | BACKGROUND: FLASH is a huge nuclear protein involved in various cellular functions such as apoptosis signalling, NF-κB activation, S-phase regulation, processing of histone pre-mRNAs, and co-regulation of transcription. Recently, we identified FLASH as a co-activator of the transcription factor c-Myb and found FLASH to be tightly associated with active transcription foci. As a huge multifunctional protein, FLASH is expected to have many interaction partners, some which may shed light on its function as a transcriptional regulator. RESULTS: To find additional FLASH-associated proteins, we performed a yeast two-hybrid (Y2H) screening with FLASH as bait and identified the SUMO E3 ligase PIAS1 as an interaction partner. The association appears to involve two distinct interaction surfaces in FLASH. We verified the interaction by Y2H-mating, GST pulldowns, co-IP and ChIP. FLASH and PIAS1 were found to co-localize in nuclear speckles. Functional assays revealed that PIAS1 enhances the intrinsic transcriptional activity of FLASH in a RING finger-dependent manner. Furthermore, PIAS1 also augments the specific activity of c-Myb, and cooperates with FLASH to further co-activate c-Myb. The three proteins, FLASH, PIAS1, and c-Myb, are all co-localized with active RNA polymerase II foci, resembling transcription factories. CONCLUSIONS: We conclude that PIAS1 is a common partner for two cancer-related nuclear factors, c-Myb and FLASH. Our results point to a functional cooperation between FLASH and PIAS1 in the enhancement of c-Myb activity in active nuclear foci. |
format | Text |
id | pubmed-3050860 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-30508602011-03-09 PIAS1 interacts with FLASH and enhances its co-activation of c-Myb Alm-Kristiansen, Anne Hege Lorenzo, Petra I Molværsmyr, Ann-Kristin Matre, Vilborg Ledsaak, Marit Sæther, Thomas Gabrielsen, Odd S Mol Cancer Research BACKGROUND: FLASH is a huge nuclear protein involved in various cellular functions such as apoptosis signalling, NF-κB activation, S-phase regulation, processing of histone pre-mRNAs, and co-regulation of transcription. Recently, we identified FLASH as a co-activator of the transcription factor c-Myb and found FLASH to be tightly associated with active transcription foci. As a huge multifunctional protein, FLASH is expected to have many interaction partners, some which may shed light on its function as a transcriptional regulator. RESULTS: To find additional FLASH-associated proteins, we performed a yeast two-hybrid (Y2H) screening with FLASH as bait and identified the SUMO E3 ligase PIAS1 as an interaction partner. The association appears to involve two distinct interaction surfaces in FLASH. We verified the interaction by Y2H-mating, GST pulldowns, co-IP and ChIP. FLASH and PIAS1 were found to co-localize in nuclear speckles. Functional assays revealed that PIAS1 enhances the intrinsic transcriptional activity of FLASH in a RING finger-dependent manner. Furthermore, PIAS1 also augments the specific activity of c-Myb, and cooperates with FLASH to further co-activate c-Myb. The three proteins, FLASH, PIAS1, and c-Myb, are all co-localized with active RNA polymerase II foci, resembling transcription factories. CONCLUSIONS: We conclude that PIAS1 is a common partner for two cancer-related nuclear factors, c-Myb and FLASH. Our results point to a functional cooperation between FLASH and PIAS1 in the enhancement of c-Myb activity in active nuclear foci. BioMed Central 2011-02-21 /pmc/articles/PMC3050860/ /pubmed/21338522 http://dx.doi.org/10.1186/1476-4598-10-21 Text en Copyright ©2011 Alm-Kristiansen et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Alm-Kristiansen, Anne Hege Lorenzo, Petra I Molværsmyr, Ann-Kristin Matre, Vilborg Ledsaak, Marit Sæther, Thomas Gabrielsen, Odd S PIAS1 interacts with FLASH and enhances its co-activation of c-Myb |
title | PIAS1 interacts with FLASH and enhances its co-activation of c-Myb |
title_full | PIAS1 interacts with FLASH and enhances its co-activation of c-Myb |
title_fullStr | PIAS1 interacts with FLASH and enhances its co-activation of c-Myb |
title_full_unstemmed | PIAS1 interacts with FLASH and enhances its co-activation of c-Myb |
title_short | PIAS1 interacts with FLASH and enhances its co-activation of c-Myb |
title_sort | pias1 interacts with flash and enhances its co-activation of c-myb |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3050860/ https://www.ncbi.nlm.nih.gov/pubmed/21338522 http://dx.doi.org/10.1186/1476-4598-10-21 |
work_keys_str_mv | AT almkristiansenannehege pias1interactswithflashandenhancesitscoactivationofcmyb AT lorenzopetrai pias1interactswithflashandenhancesitscoactivationofcmyb AT molværsmyrannkristin pias1interactswithflashandenhancesitscoactivationofcmyb AT matrevilborg pias1interactswithflashandenhancesitscoactivationofcmyb AT ledsaakmarit pias1interactswithflashandenhancesitscoactivationofcmyb AT sætherthomas pias1interactswithflashandenhancesitscoactivationofcmyb AT gabrielsenodds pias1interactswithflashandenhancesitscoactivationofcmyb |