Regulating the regulators: Serine/arginine-rich proteins under scrutiny

Serine/arginine-rich (SR) proteins are among the most studied splicing regulators. They constitute a family of evolutionarily conserved proteins that, apart from their initially identified and deeply studied role in splicing regulation, have been implicated in genome stability, chromatin binding, tr...

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Detalles Bibliográficos
Autores principales: Risso, G., Pelisch, F., Quaglino, A., Pozzi, B., Srebrow, A.
Formato: JOUR
Materias:
alternative splicing
eukaryotic gene expression
pre-mRNA processing
protein expression
protein function
messenger RNA
protein arginine methyltransferase
serine arginine rich protein
SUMO protein
acetylation
biogenesis
human
mammal cell
methylation
molecular mechanics
protein localization
protein metabolism
protein phosphorylation
protein processing
protein stability
proteomics
review
RNA splicing
signal transduction
Alternative Splicing
Animals
Conserved Sequence
Feedback, Physiological
Gene Expression Regulation
Humans
MicroRNAs
Nuclear Proteins
Protein Biosynthesis
Protein Processing, Post-Translational
RNA, Messenger
RNA-Binding Proteins
Signal Transduction
Small Ubiquitin-Related Modifier Proteins
Eukaryota
Mammalia
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_15216543_v64_n10_p809_Risso
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_15216543_v64_n10_p809_Risso
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spelling todo:paper_15216543_v64_n10_p809_Risso2023-10-03T16:20:39Z Regulating the regulators: Serine/arginine-rich proteins under scrutiny Risso, G. Pelisch, F. Quaglino, A. Pozzi, B. Srebrow, A. alternative splicing eukaryotic gene expression pre-mRNA processing protein expression protein function messenger RNA protein arginine methyltransferase serine arginine rich protein SUMO protein acetylation biogenesis human mammal cell methylation molecular mechanics protein expression protein function protein localization protein metabolism protein phosphorylation protein processing protein stability proteomics review RNA splicing signal transduction Alternative Splicing Animals Conserved Sequence Feedback, Physiological Gene Expression Regulation Humans MicroRNAs Nuclear Proteins Protein Biosynthesis Protein Processing, Post-Translational RNA, Messenger RNA-Binding Proteins Signal Transduction Small Ubiquitin-Related Modifier Proteins Eukaryota Mammalia Serine/arginine-rich (SR) proteins are among the most studied splicing regulators. They constitute a family of evolutionarily conserved proteins that, apart from their initially identified and deeply studied role in splicing regulation, have been implicated in genome stability, chromatin binding, transcription elongation, mRNA stability, mRNA export and mRNA translation. Remarkably, this list of SR protein activities seems far from complete, as unexpected functions keep being unraveled. An intriguing aspect that awaits further investigation is how the multiple tasks of SR proteins are concertedly regulated within mammalian cells. In this article, we first discuss recent findings regarding the regulation of SR protein expression, activity and accessibility. We dive into recent studies describing SR protein auto-regulatory feedback loops involving different molecular mechanisms such asunproductive splicing, microRNA-mediated regulation and translational repression. In addition, we take into account another step of regulation of SR proteins, presenting new findings about a variety of post-translational modifications by proteomics approaches and how some of these modifications can regulate SR protein sub-cellular localization or stability. Towards the end, we focus in two recently revealed functions of SR proteins beyond mRNA biogenesis and metabolism, the regulation of micro-RNA processing and the regulation of small ubiquitin-like modifier (SUMO) conjugation. © 2012 IUBMB IUBMB Life, 64(10): 809-816, 2012 Copyright © 2012 International Union of Biochemistry and Molecular Biology, Inc. Fil:Risso, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pelisch, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Quaglino, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pozzi, B. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Srebrow, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_15216543_v64_n10_p809_Risso
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic alternative splicing
eukaryotic gene expression
pre-mRNA processing
protein expression
protein function
messenger RNA
protein arginine methyltransferase
serine arginine rich protein
SUMO protein
acetylation
biogenesis
human
mammal cell
methylation
molecular mechanics
protein expression
protein function
protein localization
protein metabolism
protein phosphorylation
protein processing
protein stability
proteomics
review
RNA splicing
signal transduction
Alternative Splicing
Animals
Conserved Sequence
Feedback, Physiological
Gene Expression Regulation
Humans
MicroRNAs
Nuclear Proteins
Protein Biosynthesis
Protein Processing, Post-Translational
RNA, Messenger
RNA-Binding Proteins
Signal Transduction
Small Ubiquitin-Related Modifier Proteins
Eukaryota
Mammalia
spellingShingle alternative splicing
eukaryotic gene expression
pre-mRNA processing
protein expression
protein function
messenger RNA
protein arginine methyltransferase
serine arginine rich protein
SUMO protein
acetylation
biogenesis
human
mammal cell
methylation
molecular mechanics
protein expression
protein function
protein localization
protein metabolism
protein phosphorylation
protein processing
protein stability
proteomics
review
RNA splicing
signal transduction
Alternative Splicing
Animals
Conserved Sequence
Feedback, Physiological
Gene Expression Regulation
Humans
MicroRNAs
Nuclear Proteins
Protein Biosynthesis
Protein Processing, Post-Translational
RNA, Messenger
RNA-Binding Proteins
Signal Transduction
Small Ubiquitin-Related Modifier Proteins
Eukaryota
Mammalia
Risso, G.
Pelisch, F.
Quaglino, A.
Pozzi, B.
Srebrow, A.
Regulating the regulators: Serine/arginine-rich proteins under scrutiny
topic_facet alternative splicing
eukaryotic gene expression
pre-mRNA processing
protein expression
protein function
messenger RNA
protein arginine methyltransferase
serine arginine rich protein
SUMO protein
acetylation
biogenesis
human
mammal cell
methylation
molecular mechanics
protein expression
protein function
protein localization
protein metabolism
protein phosphorylation
protein processing
protein stability
proteomics
review
RNA splicing
signal transduction
Alternative Splicing
Animals
Conserved Sequence
Feedback, Physiological
Gene Expression Regulation
Humans
MicroRNAs
Nuclear Proteins
Protein Biosynthesis
Protein Processing, Post-Translational
RNA, Messenger
RNA-Binding Proteins
Signal Transduction
Small Ubiquitin-Related Modifier Proteins
Eukaryota
Mammalia
description Serine/arginine-rich (SR) proteins are among the most studied splicing regulators. They constitute a family of evolutionarily conserved proteins that, apart from their initially identified and deeply studied role in splicing regulation, have been implicated in genome stability, chromatin binding, transcription elongation, mRNA stability, mRNA export and mRNA translation. Remarkably, this list of SR protein activities seems far from complete, as unexpected functions keep being unraveled. An intriguing aspect that awaits further investigation is how the multiple tasks of SR proteins are concertedly regulated within mammalian cells. In this article, we first discuss recent findings regarding the regulation of SR protein expression, activity and accessibility. We dive into recent studies describing SR protein auto-regulatory feedback loops involving different molecular mechanisms such asunproductive splicing, microRNA-mediated regulation and translational repression. In addition, we take into account another step of regulation of SR proteins, presenting new findings about a variety of post-translational modifications by proteomics approaches and how some of these modifications can regulate SR protein sub-cellular localization or stability. Towards the end, we focus in two recently revealed functions of SR proteins beyond mRNA biogenesis and metabolism, the regulation of micro-RNA processing and the regulation of small ubiquitin-like modifier (SUMO) conjugation. © 2012 IUBMB IUBMB Life, 64(10): 809-816, 2012 Copyright © 2012 International Union of Biochemistry and Molecular Biology, Inc.
format JOUR
author Risso, G.
Pelisch, F.
Quaglino, A.
Pozzi, B.
Srebrow, A.
author_facet Risso, G.
Pelisch, F.
Quaglino, A.
Pozzi, B.
Srebrow, A.
author_sort Risso, G.
title Regulating the regulators: Serine/arginine-rich proteins under scrutiny
title_short Regulating the regulators: Serine/arginine-rich proteins under scrutiny
title_full Regulating the regulators: Serine/arginine-rich proteins under scrutiny
title_fullStr Regulating the regulators: Serine/arginine-rich proteins under scrutiny
title_full_unstemmed Regulating the regulators: Serine/arginine-rich proteins under scrutiny
title_sort regulating the regulators: serine/arginine-rich proteins under scrutiny
url http://hdl.handle.net/20.500.12110/paper_15216543_v64_n10_p809_Risso
work_keys_str_mv AT rissog regulatingtheregulatorsserineargininerichproteinsunderscrutiny
AT pelischf regulatingtheregulatorsserineargininerichproteinsunderscrutiny
AT quaglinoa regulatingtheregulatorsserineargininerichproteinsunderscrutiny
AT pozzib regulatingtheregulatorsserineargininerichproteinsunderscrutiny
AT srebrowa regulatingtheregulatorsserineargininerichproteinsunderscrutiny
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