Identification of novel PANDAR protein interaction partners involved in splicing regulation

Abstract Interactions of long non-coding RNAs (lncRNA) with proteins play important roles in the regulation of many cellular processes. PANDAR (Promotor of CDKN1A Antisense DNA damage Activated RNA) is a lncRNA that is transcribed in a p53-dependent manner from the CDKN1A promoter and is involved in...

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Autores principales:	N. Pospiech, H. Cibis, L. Dietrich, F. Müller, T. Bange, S. Hennig
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7d70090ebdd14b8a9d41769111f03876
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spelling	oai:doaj.org-article:7d70090ebdd14b8a9d41769111f038762021-12-02T15:08:17ZIdentification of novel PANDAR protein interaction partners involved in splicing regulation10.1038/s41598-018-21105-62045-2322https://doaj.org/article/7d70090ebdd14b8a9d41769111f038762018-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-21105-6https://doaj.org/toc/2045-2322Abstract Interactions of long non-coding RNAs (lncRNA) with proteins play important roles in the regulation of many cellular processes. PANDAR (Promotor of CDKN1A Antisense DNA damage Activated RNA) is a lncRNA that is transcribed in a p53-dependent manner from the CDKN1A promoter and is involved in the regulation of proliferation and senescence. Overexpression of PANDAR has been observed in several tumor species and correlated with a poor prognosis for patient survival rate. Depending on the cellular state, PANDAR is known to interact with proteins such as the nuclear transcription factor Y subunit A (NF-YA) and the scaffold attachment factor A (SAF-A). However, a comprehensive analysis of the PANDAR interactome was missing so far. Therefore, we applied peptide nucleic acid (PNA)-based pull-downs combined with quantitative mass spectrometry to identify new protein binding partners. We confirmed potential candidates like U2AF65 and PTBP1, known to be involved in RNA processing. Furthermore, we observed that overexpression of PANDAR leads to a reduced level of the short pro-apoptotic BCL-X splice variant (BCL-XS) which is regulated by PTBP1. Simultaneous overexpression of PTBP1 was able to rescue this effect. Overall, our data suggest a role for PANDAR in the regulation of splicing events via its interaction partner PTBP1.N. PospiechH. CibisL. DietrichF. MüllerT. BangeS. HennigNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-9 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q N. Pospiech H. Cibis L. Dietrich F. Müller T. Bange S. Hennig Identification of novel PANDAR protein interaction partners involved in splicing regulation
description	Abstract Interactions of long non-coding RNAs (lncRNA) with proteins play important roles in the regulation of many cellular processes. PANDAR (Promotor of CDKN1A Antisense DNA damage Activated RNA) is a lncRNA that is transcribed in a p53-dependent manner from the CDKN1A promoter and is involved in the regulation of proliferation and senescence. Overexpression of PANDAR has been observed in several tumor species and correlated with a poor prognosis for patient survival rate. Depending on the cellular state, PANDAR is known to interact with proteins such as the nuclear transcription factor Y subunit A (NF-YA) and the scaffold attachment factor A (SAF-A). However, a comprehensive analysis of the PANDAR interactome was missing so far. Therefore, we applied peptide nucleic acid (PNA)-based pull-downs combined with quantitative mass spectrometry to identify new protein binding partners. We confirmed potential candidates like U2AF65 and PTBP1, known to be involved in RNA processing. Furthermore, we observed that overexpression of PANDAR leads to a reduced level of the short pro-apoptotic BCL-X splice variant (BCL-XS) which is regulated by PTBP1. Simultaneous overexpression of PTBP1 was able to rescue this effect. Overall, our data suggest a role for PANDAR in the regulation of splicing events via its interaction partner PTBP1.
format	article
author	N. Pospiech H. Cibis L. Dietrich F. Müller T. Bange S. Hennig
author_facet	N. Pospiech H. Cibis L. Dietrich F. Müller T. Bange S. Hennig
author_sort	N. Pospiech
title	Identification of novel PANDAR protein interaction partners involved in splicing regulation
title_short	Identification of novel PANDAR protein interaction partners involved in splicing regulation
title_full	Identification of novel PANDAR protein interaction partners involved in splicing regulation
title_fullStr	Identification of novel PANDAR protein interaction partners involved in splicing regulation
title_full_unstemmed	Identification of novel PANDAR protein interaction partners involved in splicing regulation
title_sort	identification of novel pandar protein interaction partners involved in splicing regulation
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/7d70090ebdd14b8a9d41769111f03876
work_keys_str_mv	AT npospiech identificationofnovelpandarproteininteractionpartnersinvolvedinsplicingregulation AT hcibis identificationofnovelpandarproteininteractionpartnersinvolvedinsplicingregulation AT ldietrich identificationofnovelpandarproteininteractionpartnersinvolvedinsplicingregulation AT fmuller identificationofnovelpandarproteininteractionpartnersinvolvedinsplicingregulation AT tbange identificationofnovelpandarproteininteractionpartnersinvolvedinsplicingregulation AT shennig identificationofnovelpandarproteininteractionpartnersinvolvedinsplicingregulation
_version_	1718388197046616064

Identification of novel PANDAR protein interaction partners involved in splicing regulation

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