The tandem Agenet domain of fragile X mental retardation protein interacts with FUS

Abstract The tandem Agenet domain (TAD) of fragile X mental retardation protein (FMRP) protein is considered to be a member of the methyl-lysine-binding Tudor domain “Royal family”. Several groups have reported that the TAD binds with methylated histones and plays a role in DNA damage responses. FMR...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Qingzhong He, Wei Ge
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/865e98d5f01d4383be16758cef6390c4
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:865e98d5f01d4383be16758cef6390c4
record_format	dspace
spelling	oai:doaj.org-article:865e98d5f01d4383be16758cef6390c42021-12-02T12:32:24ZThe tandem Agenet domain of fragile X mental retardation protein interacts with FUS10.1038/s41598-017-01175-82045-2322https://doaj.org/article/865e98d5f01d4383be16758cef6390c42017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01175-8https://doaj.org/toc/2045-2322Abstract The tandem Agenet domain (TAD) of fragile X mental retardation protein (FMRP) protein is considered to be a member of the methyl-lysine-binding Tudor domain “Royal family”. Several groups have reported that the TAD binds with methylated histones and plays a role in DNA damage responses. FMRP is a RNA-binding protein predominantly resident in cytoplasm. Therefore, in this study, we identified DDX5, FUS, EWSR1 and LSM14A as TAD-interacting proteins sensitive to F32L and/or Y96L mutation by pull-down assays and mass spectrometry. We also showed that the interaction is potentially mediated by RGG/RG motifs. Furthermore, when FMRP was knocked-down, translocation of exogenously expressed wild-type FUS and disease-related mutant R514G was observed. This study may provide a novel insight into FMRP involvement in the intracellular localization of FUS and pathology of FUS-related amyotrophic lateral sclerosis.Qingzhong HeWei GeNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-7 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Qingzhong He Wei Ge The tandem Agenet domain of fragile X mental retardation protein interacts with FUS
description	Abstract The tandem Agenet domain (TAD) of fragile X mental retardation protein (FMRP) protein is considered to be a member of the methyl-lysine-binding Tudor domain “Royal family”. Several groups have reported that the TAD binds with methylated histones and plays a role in DNA damage responses. FMRP is a RNA-binding protein predominantly resident in cytoplasm. Therefore, in this study, we identified DDX5, FUS, EWSR1 and LSM14A as TAD-interacting proteins sensitive to F32L and/or Y96L mutation by pull-down assays and mass spectrometry. We also showed that the interaction is potentially mediated by RGG/RG motifs. Furthermore, when FMRP was knocked-down, translocation of exogenously expressed wild-type FUS and disease-related mutant R514G was observed. This study may provide a novel insight into FMRP involvement in the intracellular localization of FUS and pathology of FUS-related amyotrophic lateral sclerosis.
format	article
author	Qingzhong He Wei Ge
author_facet	Qingzhong He Wei Ge
author_sort	Qingzhong He
title	The tandem Agenet domain of fragile X mental retardation protein interacts with FUS
title_short	The tandem Agenet domain of fragile X mental retardation protein interacts with FUS
title_full	The tandem Agenet domain of fragile X mental retardation protein interacts with FUS
title_fullStr	The tandem Agenet domain of fragile X mental retardation protein interacts with FUS
title_full_unstemmed	The tandem Agenet domain of fragile X mental retardation protein interacts with FUS
title_sort	tandem agenet domain of fragile x mental retardation protein interacts with fus
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/865e98d5f01d4383be16758cef6390c4
work_keys_str_mv	AT qingzhonghe thetandemagenetdomainoffragilexmentalretardationproteininteractswithfus AT weige thetandemagenetdomainoffragilexmentalretardationproteininteractswithfus AT qingzhonghe tandemagenetdomainoffragilexmentalretardationproteininteractswithfus AT weige tandemagenetdomainoffragilexmentalretardationproteininteractswithfus
_version_	1718394104966021120

The tandem Agenet domain of fragile X mental retardation protein interacts with FUS

Ejemplares similares