RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site

Summary: Fragile X-related protein-1 (FXR1) gene is highly amplified in patients with ovarian cancer, and this amplification is associated with increased expression of both FXR1 mRNA and protein. FXR1 expression directly associates with the survival and proliferation of cancer cells. Surface sensing...

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Autores principales:	Jasmine George, Yongsheng Li, Ishaque P. Kadamberi, Deepak Parashar, Shirng-Wern Tsaih, Prachi Gupta, Anjali Geethadevi, Changliang Chen, Chandrima Ghosh, Yunguang Sun, Sonam Mittal, Ramani Ramchandran, Hallgeir Rui, Gabriel Lopez-Berestein, Cristian Rodriguez-Aguayo, Gustavo Leone, Janet S. Rader, Anil K. Sood, Madhusudan Dey, Sunila Pradeep, Pradeep Chaluvally-Raghavan
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	FXR1 ovarian cancer cMYC SUnSET eIFs ARE Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/1bda5605c1c8465997ff1e6038dd99f9
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spelling	oai:doaj.org-article:1bda5605c1c8465997ff1e6038dd99f92021-11-04T04:29:23ZRNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site2211-124710.1016/j.celrep.2021.109934https://doaj.org/article/1bda5605c1c8465997ff1e6038dd99f92021-11-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2211124721014078https://doaj.org/toc/2211-1247Summary: Fragile X-related protein-1 (FXR1) gene is highly amplified in patients with ovarian cancer, and this amplification is associated with increased expression of both FXR1 mRNA and protein. FXR1 expression directly associates with the survival and proliferation of cancer cells. Surface sensing of translation (SUnSET) assay demonstrates that FXR1 enhances the overall translation in cancer cells. Reverse-phase protein array (RPPA) reveals that cMYC is the key target of FXR1. Mechanistically, FXR1 binds to the AU-rich elements (ARE) present within the 3′ untranslated region (3′UTR) of cMYC and stabilizes its expression. In addition, the RGG domain in FXR1 interacts with eIF4A1 and eIF4E proteins. These two interactions of FXR1 result in the circularization of cMYC mRNA and facilitate the recruitment of eukaryotic translation initiation factors to the translation start site. In brief, we uncover a mechanism by which FXR1 promotes cMYC levels in cancer cells.Jasmine GeorgeYongsheng LiIshaque P. KadamberiDeepak ParasharShirng-Wern TsaihPrachi GuptaAnjali GeethadeviChangliang ChenChandrima GhoshYunguang SunSonam MittalRamani RamchandranHallgeir RuiGabriel Lopez-BeresteinCristian Rodriguez-AguayoGustavo LeoneJanet S. RaderAnil K. SoodMadhusudan DeySunila PradeepPradeep Chaluvally-RaghavanElsevierarticleFXR1ovarian cancercMYCSUnSETeIFsAREBiology (General)QH301-705.5ENCell Reports, Vol 37, Iss 5, Pp 109934- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	FXR1 ovarian cancer cMYC SUnSET eIFs ARE Biology (General) QH301-705.5
spellingShingle	FXR1 ovarian cancer cMYC SUnSET eIFs ARE Biology (General) QH301-705.5 Jasmine George Yongsheng Li Ishaque P. Kadamberi Deepak Parashar Shirng-Wern Tsaih Prachi Gupta Anjali Geethadevi Changliang Chen Chandrima Ghosh Yunguang Sun Sonam Mittal Ramani Ramchandran Hallgeir Rui Gabriel Lopez-Berestein Cristian Rodriguez-Aguayo Gustavo Leone Janet S. Rader Anil K. Sood Madhusudan Dey Sunila Pradeep Pradeep Chaluvally-Raghavan RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site
description	Summary: Fragile X-related protein-1 (FXR1) gene is highly amplified in patients with ovarian cancer, and this amplification is associated with increased expression of both FXR1 mRNA and protein. FXR1 expression directly associates with the survival and proliferation of cancer cells. Surface sensing of translation (SUnSET) assay demonstrates that FXR1 enhances the overall translation in cancer cells. Reverse-phase protein array (RPPA) reveals that cMYC is the key target of FXR1. Mechanistically, FXR1 binds to the AU-rich elements (ARE) present within the 3′ untranslated region (3′UTR) of cMYC and stabilizes its expression. In addition, the RGG domain in FXR1 interacts with eIF4A1 and eIF4E proteins. These two interactions of FXR1 result in the circularization of cMYC mRNA and facilitate the recruitment of eukaryotic translation initiation factors to the translation start site. In brief, we uncover a mechanism by which FXR1 promotes cMYC levels in cancer cells.
format	article
author	Jasmine George Yongsheng Li Ishaque P. Kadamberi Deepak Parashar Shirng-Wern Tsaih Prachi Gupta Anjali Geethadevi Changliang Chen Chandrima Ghosh Yunguang Sun Sonam Mittal Ramani Ramchandran Hallgeir Rui Gabriel Lopez-Berestein Cristian Rodriguez-Aguayo Gustavo Leone Janet S. Rader Anil K. Sood Madhusudan Dey Sunila Pradeep Pradeep Chaluvally-Raghavan
author_facet	Jasmine George Yongsheng Li Ishaque P. Kadamberi Deepak Parashar Shirng-Wern Tsaih Prachi Gupta Anjali Geethadevi Changliang Chen Chandrima Ghosh Yunguang Sun Sonam Mittal Ramani Ramchandran Hallgeir Rui Gabriel Lopez-Berestein Cristian Rodriguez-Aguayo Gustavo Leone Janet S. Rader Anil K. Sood Madhusudan Dey Sunila Pradeep Pradeep Chaluvally-Raghavan
author_sort	Jasmine George
title	RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site
title_short	RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site
title_full	RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site
title_fullStr	RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site
title_full_unstemmed	RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site
title_sort	rna-binding protein fxr1 drives cmyc translation by recruiting eif4f complex to the translation start site
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/1bda5605c1c8465997ff1e6038dd99f9
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RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site

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