Staufen: From embryo polarity to cellular stress and neurodegeneration

Staufen is a double-stranded RNA-binding protein that forms RNA granules by RNA-dependent and - independent interactions. Staufen was initially described in Drosophila as a key molecule for targeting maternal mRNAs. In vertebrates, two highly similar paralogs with several splicing variants mediate m...

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Autores principales:	Thomas, María Gabriela, Baez, María Verónica, Chernomoretz, Ariel, Boccaccio, Graciela Lidia
Publicado:	2012
Materias:	FMRP FUS/TLS/hnRNP P2 HIV Huntingtin Influenza virus Memory Mrna transport Neurodegeneration Neuron Oligodendrocyte Review SCA8 Staufen Stress granules TDP-43 apolipoprotein B messenger RNA editing enzyme catalytic polypeptide 3G double stranded RNA fragile X mental retardation protein fused in sarcoma protein huntingtin messenger RNA nucleic acid binding protein protein kinase R ribonucleoprotein RNA binding protein spinocerebellar ataxia 8 protein staufen 1 protein staufen 2 protein TAR DNA binding protein unclassified drug virus protein virus RNA messenger ribonucleoprotein RNA alternative RNA splicing article cell granule cell stress cell survival cellular distribution dendrite dendritic spine Drosophila Duchenne muscular dystrophy embryo polarity enzyme activation enzyme activity gene deletion gene overexpression gene silencing human Human immunodeficiency virus 1 Influenza virus A learning memory morphogenesis myotonic dystrophy nerve cell plasticity nerve degeneration nonhuman nucleotide repeat oligodendroglia oxidative stress polysome protein synthesis RNA binding rna silencing RNA stability RNA structure RNA transport spine spine morphogenesis spinocerebellar ataxia 2 spinocerebellar degeneration stress granule synapse translation regulation vertebrate virus assembly virus particle animal genetics metabolism physiology review Animals Humans Ribonucleoproteins RNA Stability RNA Transport RNA, Messenger RNA-Binding Proteins
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19450516_v4S_n2_p432_Tosar http://hdl.handle.net/20.500.12110/paper_19450516_v4S_n2_p432_Tosar
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	paper:paper_19450516_v4S_n2_p432_Tosar2023-06-08T16:32:29Z Staufen: From embryo polarity to cellular stress and neurodegeneration Thomas, María Gabriela Baez, María Verónica Chernomoretz, Ariel Boccaccio, Graciela Lidia FMRP FUS/TLS/hnRNP P2 HIV Huntingtin Influenza virus Memory Mrna transport Neurodegeneration Neuron Oligodendrocyte Review SCA8 Staufen Stress granules TDP-43 apolipoprotein B messenger RNA editing enzyme catalytic polypeptide 3G double stranded RNA fragile X mental retardation protein fused in sarcoma protein huntingtin messenger RNA nucleic acid binding protein protein kinase R ribonucleoprotein RNA binding protein spinocerebellar ataxia 8 protein staufen 1 protein staufen 2 protein TAR DNA binding protein unclassified drug virus protein virus RNA messenger ribonucleoprotein messenger RNA ribonucleoprotein RNA RNA binding protein alternative RNA splicing article cell granule cell stress cell survival cellular distribution dendrite dendritic spine Drosophila Duchenne muscular dystrophy embryo polarity enzyme activation enzyme activity gene deletion gene overexpression gene silencing human Human immunodeficiency virus 1 Influenza virus A learning memory morphogenesis myotonic dystrophy nerve cell plasticity nerve degeneration nonhuman nucleotide repeat oligodendroglia oxidative stress polysome protein synthesis RNA binding rna silencing RNA stability RNA structure RNA transport spine spine morphogenesis spinocerebellar ataxia 2 spinocerebellar degeneration stress granule synapse translation regulation vertebrate virus assembly virus particle animal genetics metabolism physiology review Animals Humans Ribonucleoproteins RNA RNA Stability RNA Transport RNA, Messenger RNA-Binding Proteins Staufen is a double-stranded RNA-binding protein that forms RNA granules by RNA-dependent and - independent interactions. Staufen was initially described in Drosophila as a key molecule for targeting maternal mRNAs. In vertebrates, two highly similar paralogs with several splicing variants mediate mRNA transport, thus affecting neuron plasticity, learning and memory. Staufen also regulates translation and mRNA decay. In recent years, Staufen was shown to be an important regulatory component of stress granules (SGs), which are large aggregates of silenced mRNPs specifically induced upon acute cellular stress. SGs contribute to cell survival by reprogramming translation and inhibiting pro-apoptotic pathways, and Staufen appears to negatively modulate SG formation by several mechanisms. More recently, mammalian Staufen was found in RNA granules and pathological cytoplasmic aggregates related to SGs containing huntingtin, TDP43, FUS/TLS or FMRP. In addition, Staufen binds CUG repeats present in mutant RNAs causative of degenerative conditions, thus ameliorating disease. Finally, Staufen affects HIV and influenza infection at several levels. Collectively, these observations unveil important roles for Staufen-mediated post-transcriptional regulation in a growing number of human diseases. Fil:Thomas, M.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Baez, M.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Chernomoretz, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Boccaccio, G.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19450516_v4S_n2_p432_Tosar http://hdl.handle.net/20.500.12110/paper_19450516_v4S_n2_p432_Tosar
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	FMRP FUS/TLS/hnRNP P2 HIV Huntingtin Influenza virus Memory Mrna transport Neurodegeneration Neuron Oligodendrocyte Review SCA8 Staufen Stress granules TDP-43 apolipoprotein B messenger RNA editing enzyme catalytic polypeptide 3G double stranded RNA fragile X mental retardation protein fused in sarcoma protein huntingtin messenger RNA nucleic acid binding protein protein kinase R ribonucleoprotein RNA binding protein spinocerebellar ataxia 8 protein staufen 1 protein staufen 2 protein TAR DNA binding protein unclassified drug virus protein virus RNA messenger ribonucleoprotein messenger RNA ribonucleoprotein RNA RNA binding protein alternative RNA splicing article cell granule cell stress cell survival cellular distribution dendrite dendritic spine Drosophila Duchenne muscular dystrophy embryo polarity enzyme activation enzyme activity gene deletion gene overexpression gene silencing human Human immunodeficiency virus 1 Influenza virus A learning memory morphogenesis myotonic dystrophy nerve cell plasticity nerve degeneration nonhuman nucleotide repeat oligodendroglia oxidative stress polysome protein synthesis RNA binding rna silencing RNA stability RNA structure RNA transport spine spine morphogenesis spinocerebellar ataxia 2 spinocerebellar degeneration stress granule synapse translation regulation vertebrate virus assembly virus particle animal genetics metabolism physiology review Animals Humans Ribonucleoproteins RNA RNA Stability RNA Transport RNA, Messenger RNA-Binding Proteins
spellingShingle	FMRP FUS/TLS/hnRNP P2 HIV Huntingtin Influenza virus Memory Mrna transport Neurodegeneration Neuron Oligodendrocyte Review SCA8 Staufen Stress granules TDP-43 apolipoprotein B messenger RNA editing enzyme catalytic polypeptide 3G double stranded RNA fragile X mental retardation protein fused in sarcoma protein huntingtin messenger RNA nucleic acid binding protein protein kinase R ribonucleoprotein RNA binding protein spinocerebellar ataxia 8 protein staufen 1 protein staufen 2 protein TAR DNA binding protein unclassified drug virus protein virus RNA messenger ribonucleoprotein messenger RNA ribonucleoprotein RNA RNA binding protein alternative RNA splicing article cell granule cell stress cell survival cellular distribution dendrite dendritic spine Drosophila Duchenne muscular dystrophy embryo polarity enzyme activation enzyme activity gene deletion gene overexpression gene silencing human Human immunodeficiency virus 1 Influenza virus A learning memory morphogenesis myotonic dystrophy nerve cell plasticity nerve degeneration nonhuman nucleotide repeat oligodendroglia oxidative stress polysome protein synthesis RNA binding rna silencing RNA stability RNA structure RNA transport spine spine morphogenesis spinocerebellar ataxia 2 spinocerebellar degeneration stress granule synapse translation regulation vertebrate virus assembly virus particle animal genetics metabolism physiology review Animals Humans Ribonucleoproteins RNA RNA Stability RNA Transport RNA, Messenger RNA-Binding Proteins Thomas, María Gabriela Baez, María Verónica Chernomoretz, Ariel Boccaccio, Graciela Lidia Staufen: From embryo polarity to cellular stress and neurodegeneration
topic_facet	FMRP FUS/TLS/hnRNP P2 HIV Huntingtin Influenza virus Memory Mrna transport Neurodegeneration Neuron Oligodendrocyte Review SCA8 Staufen Stress granules TDP-43 apolipoprotein B messenger RNA editing enzyme catalytic polypeptide 3G double stranded RNA fragile X mental retardation protein fused in sarcoma protein huntingtin messenger RNA nucleic acid binding protein protein kinase R ribonucleoprotein RNA binding protein spinocerebellar ataxia 8 protein staufen 1 protein staufen 2 protein TAR DNA binding protein unclassified drug virus protein virus RNA messenger ribonucleoprotein messenger RNA ribonucleoprotein RNA RNA binding protein alternative RNA splicing article cell granule cell stress cell survival cellular distribution dendrite dendritic spine Drosophila Duchenne muscular dystrophy embryo polarity enzyme activation enzyme activity gene deletion gene overexpression gene silencing human Human immunodeficiency virus 1 Influenza virus A learning memory morphogenesis myotonic dystrophy nerve cell plasticity nerve degeneration nonhuman nucleotide repeat oligodendroglia oxidative stress polysome protein synthesis RNA binding rna silencing RNA stability RNA structure RNA transport spine spine morphogenesis spinocerebellar ataxia 2 spinocerebellar degeneration stress granule synapse translation regulation vertebrate virus assembly virus particle animal genetics metabolism physiology review Animals Humans Ribonucleoproteins RNA RNA Stability RNA Transport RNA, Messenger RNA-Binding Proteins
description	Staufen is a double-stranded RNA-binding protein that forms RNA granules by RNA-dependent and - independent interactions. Staufen was initially described in Drosophila as a key molecule for targeting maternal mRNAs. In vertebrates, two highly similar paralogs with several splicing variants mediate mRNA transport, thus affecting neuron plasticity, learning and memory. Staufen also regulates translation and mRNA decay. In recent years, Staufen was shown to be an important regulatory component of stress granules (SGs), which are large aggregates of silenced mRNPs specifically induced upon acute cellular stress. SGs contribute to cell survival by reprogramming translation and inhibiting pro-apoptotic pathways, and Staufen appears to negatively modulate SG formation by several mechanisms. More recently, mammalian Staufen was found in RNA granules and pathological cytoplasmic aggregates related to SGs containing huntingtin, TDP43, FUS/TLS or FMRP. In addition, Staufen binds CUG repeats present in mutant RNAs causative of degenerative conditions, thus ameliorating disease. Finally, Staufen affects HIV and influenza infection at several levels. Collectively, these observations unveil important roles for Staufen-mediated post-transcriptional regulation in a growing number of human diseases.
author	Thomas, María Gabriela Baez, María Verónica Chernomoretz, Ariel Boccaccio, Graciela Lidia
author_facet	Thomas, María Gabriela Baez, María Verónica Chernomoretz, Ariel Boccaccio, Graciela Lidia
author_sort	Thomas, María Gabriela
title	Staufen: From embryo polarity to cellular stress and neurodegeneration
title_short	Staufen: From embryo polarity to cellular stress and neurodegeneration
title_full	Staufen: From embryo polarity to cellular stress and neurodegeneration
title_fullStr	Staufen: From embryo polarity to cellular stress and neurodegeneration
title_full_unstemmed	Staufen: From embryo polarity to cellular stress and neurodegeneration
title_sort	staufen: from embryo polarity to cellular stress and neurodegeneration
publishDate	2012
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19450516_v4S_n2_p432_Tosar http://hdl.handle.net/20.500.12110/paper_19450516_v4S_n2_p432_Tosar
work_keys_str_mv	AT thomasmariagabriela staufenfromembryopolaritytocellularstressandneurodegeneration AT baezmariaveronica staufenfromembryopolaritytocellularstressandneurodegeneration AT chernomoretzariel staufenfromembryopolaritytocellularstressandneurodegeneration AT boccacciogracielalidia staufenfromembryopolaritytocellularstressandneurodegeneration
_version_	1768542524154052608

Staufen: From embryo polarity to cellular stress and neurodegeneration

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