hnRNPA3 regulates hESCs pluripotency through modulating mRNA export
Objective To explore the biological function of RNA binding protein heterogeneous nuclear ribonucleoprotein A3(hnRNPA3) in the maintenance of pluripotency of human embryonic stem cells(hESCs) and to reveal its new mechanism in RNA transport. Methods The interaction of hnRNPA3 with nuclear pore and...
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| Format: | Article |
| Language: | zho |
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Institute of Basic Medical Sciences and Peking Union Medical College Hospital, Chinese Academy of Medical Sciences / Peking Union Medical College.
2021-06-01
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| Series: | Jichu yixue yu linchuang |
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| Online Access: | http://journal11.magtechjournal.com/Jwk_jcyxylc/fileup/1001-6325/PDF/a210083.pdf |
| _version_ | 1797365827877470208 |
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| author | YANG Jia-bin, CHEN Zhong-yang, ZHOU Fan-qi, YU Jia, MA Yan-ni |
| author_facet | YANG Jia-bin, CHEN Zhong-yang, ZHOU Fan-qi, YU Jia, MA Yan-ni |
| author_sort | YANG Jia-bin, CHEN Zhong-yang, ZHOU Fan-qi, YU Jia, MA Yan-ni |
| collection | DOAJ |
| description | Objective To explore the biological function of RNA binding protein heterogeneous nuclear ribonucleoprotein A3(hnRNPA3) in the maintenance of pluripotency of human embryonic stem cells(hESCs) and to reveal its new mechanism in RNA transport. Methods The interaction of hnRNPA3 with nuclear pore and localization were examined by immunoprecipitation of nuclear pore complex and cytoplasmic separation in hESCs. After inhibiting the endogenous expression of hnRNPA3, the expression of the pluripotency/differentiation marker genes was detected by qPCR, and the effect on the nucleoplasmic distribution of polyA+ RNA and OCT4 mRNA was tested by RNA fluorescence in situ hybridization to predict the binding of hnRNPA3 to known RNA export associated proteins. Results hnRNPA3 was localized in the nucleus and interacted with the nuclear pore. Inhibiting the endogenous expression of hnRNPA3 significantly inhibited the cloning-formation ability of hESC(P＜0.05) and resulted in the increase of the expression of cell differentiation markers(P＜0.001) and significantly inhibited the export of polyA+ RNA as well as OCT4 mRNA(P＜0.001). The protein interaction network predicted that hnRNPA3 may bind to about one-third of the known RNA export associated proteins. Conclusions hnRNPA3 regulates hESC pluripotency by impacting on mRNA export. |
| first_indexed | 2024-03-08T16:54:29Z |
| format | Article |
| id | doaj.art-f815d526de09461d81da06501e284e0e |
| institution | Directory Open Access Journal |
| issn | 1001-6325 |
| language | zho |
| last_indexed | 2024-03-08T16:54:29Z |
| publishDate | 2021-06-01 |
| publisher | Institute of Basic Medical Sciences and Peking Union Medical College Hospital, Chinese Academy of Medical Sciences / Peking Union Medical College. |
| record_format | Article |
| series | Jichu yixue yu linchuang |
| spelling | doaj.art-f815d526de09461d81da06501e284e0e2024-01-05T03:05:20ZzhoInstitute of Basic Medical Sciences and Peking Union Medical College Hospital, Chinese Academy of Medical Sciences / Peking Union Medical College.Jichu yixue yu linchuang1001-63252021-06-01416811817hnRNPA3 regulates hESCs pluripotency through modulating mRNA exportYANG Jia-bin, CHEN Zhong-yang, ZHOU Fan-qi, YU Jia, MA Yan-ni0State Key Laboratory of Medical Molecular Biology, Department of Biochemistry and Molecular Biology, Institute of Basic Medicine Sciences CAMS, School of Basic Medicine PUMC, Beijing 100005, ChinaObjective To explore the biological function of RNA binding protein heterogeneous nuclear ribonucleoprotein A3(hnRNPA3) in the maintenance of pluripotency of human embryonic stem cells(hESCs) and to reveal its new mechanism in RNA transport. Methods The interaction of hnRNPA3 with nuclear pore and localization were examined by immunoprecipitation of nuclear pore complex and cytoplasmic separation in hESCs. After inhibiting the endogenous expression of hnRNPA3, the expression of the pluripotency/differentiation marker genes was detected by qPCR, and the effect on the nucleoplasmic distribution of polyA+ RNA and OCT4 mRNA was tested by RNA fluorescence in situ hybridization to predict the binding of hnRNPA3 to known RNA export associated proteins. Results hnRNPA3 was localized in the nucleus and interacted with the nuclear pore. Inhibiting the endogenous expression of hnRNPA3 significantly inhibited the cloning-formation ability of hESC(P＜0.05) and resulted in the increase of the expression of cell differentiation markers(P＜0.001) and significantly inhibited the export of polyA+ RNA as well as OCT4 mRNA(P＜0.001). The protein interaction network predicted that hnRNPA3 may bind to about one-third of the known RNA export associated proteins. Conclusions hnRNPA3 regulates hESC pluripotency by impacting on mRNA export.http://journal11.magtechjournal.com/Jwk_jcyxylc/fileup/1001-6325/PDF/a210083.pdfhuman embryonic stem cells|hnrnpa3|pluripotency and self-renewal|mrna transport |
| spellingShingle | YANG Jia-bin, CHEN Zhong-yang, ZHOU Fan-qi, YU Jia, MA Yan-ni hnRNPA3 regulates hESCs pluripotency through modulating mRNA export Jichu yixue yu linchuang human embryonic stem cells|hnrnpa3|pluripotency and self-renewal|mrna transport |
| title | hnRNPA3 regulates hESCs pluripotency through modulating mRNA export |
| title_full | hnRNPA3 regulates hESCs pluripotency through modulating mRNA export |
| title_fullStr | hnRNPA3 regulates hESCs pluripotency through modulating mRNA export |
| title_full_unstemmed | hnRNPA3 regulates hESCs pluripotency through modulating mRNA export |
| title_short | hnRNPA3 regulates hESCs pluripotency through modulating mRNA export |
| title_sort | hnrnpa3 regulates hescs pluripotency through modulating mrna export |
| topic | human embryonic stem cells|hnrnpa3|pluripotency and self-renewal|mrna transport |
| url | http://journal11.magtechjournal.com/Jwk_jcyxylc/fileup/1001-6325/PDF/a210083.pdf |
| work_keys_str_mv | AT yangjiabinchenzhongyangzhoufanqiyujiamayanni hnrnpa3regulateshescspluripotencythroughmodulatingmrnaexport |