Concerted regulation of nuclear and cytoplasmic activities of SR proteins by AKT
Serine/arginine-rich (SR) proteins are important regulators of mRNA splicing. Several postsplicing activities have been described for a subset of shuttling SR proteins, including regulation of mRNA export and translation. Using the fibronectin gene to study the links between signal-transduction path...
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todo:paper_15459993_v12_n12_p1037_Blaustein2023-10-03T16:23:04Z Concerted regulation of nuclear and cytoplasmic activities of SR proteins by AKT Blaustein, M. Pelisch, F. Tanos, T. Muñoz, M.J. Wengier, D. Quadrana, L. Sanford, J.R. Muschietti, J.P. Kornblihtt, A.R. Cáceres, J.F. Coso, O.A. Srebrow, A. fibronectin growth factor phosphatidylinositol 3 kinase protein protein kinase B serine arginine rich protein transfer RNA unclassified drug alternative RNA splicing article cytoplasm human nonhuman priority journal protein expression protein function protein localization RNA translation signal transduction 1-Phosphatidylinositol 3-Kinase Amino Acid Sequence Animals Cell Nucleus Cytoplasm Fibronectins Growth Substances Humans Molecular Sequence Data Nuclear Proteins Phosphoproteins Protein Biosynthesis Proto-Oncogene Proteins c-akt RNA Splicing RNA, Messenger RNA, Small Interfering RNA-Binding Proteins Signal Transduction Serine/arginine-rich (SR) proteins are important regulators of mRNA splicing. Several postsplicing activities have been described for a subset of shuttling SR proteins, including regulation of mRNA export and translation. Using the fibronectin gene to study the links between signal-transduction pathways and SR protein activity, we show that growth factors not only modify the alternative splicing pattern of the fibronectin gene but also alter translation of reporter messenger RNAs in an SR protein-dependent fashion, providing two coregulated levels of isoform-specific amplification. These effects are inhibited by specific small interfering RNAs against SR proteins and are mediated by the AKT kinase, which elicits opposite effects to those evoked by overexpressing SR protein kinases CIk and SRPK. These results show how SR protein activity is modified in response to extracellular stimulation, leading to a concerted regulation of splicing and translation. © 2005 Nature Publishing Group. Fil:Blaustein, M. 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:Tanos, T. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Muñoz, M.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Wengier, D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Quadrana, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Muschietti, J.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Kornblihtt, A.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Cáceres, J.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Coso, O.A. 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_15459993_v12_n12_p1037_Blaustein |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
fibronectin growth factor phosphatidylinositol 3 kinase protein protein kinase B serine arginine rich protein transfer RNA unclassified drug alternative RNA splicing article cytoplasm human nonhuman priority journal protein expression protein function protein localization RNA translation signal transduction 1-Phosphatidylinositol 3-Kinase Amino Acid Sequence Animals Cell Nucleus Cytoplasm Fibronectins Growth Substances Humans Molecular Sequence Data Nuclear Proteins Phosphoproteins Protein Biosynthesis Proto-Oncogene Proteins c-akt RNA Splicing RNA, Messenger RNA, Small Interfering RNA-Binding Proteins Signal Transduction |
spellingShingle |
fibronectin growth factor phosphatidylinositol 3 kinase protein protein kinase B serine arginine rich protein transfer RNA unclassified drug alternative RNA splicing article cytoplasm human nonhuman priority journal protein expression protein function protein localization RNA translation signal transduction 1-Phosphatidylinositol 3-Kinase Amino Acid Sequence Animals Cell Nucleus Cytoplasm Fibronectins Growth Substances Humans Molecular Sequence Data Nuclear Proteins Phosphoproteins Protein Biosynthesis Proto-Oncogene Proteins c-akt RNA Splicing RNA, Messenger RNA, Small Interfering RNA-Binding Proteins Signal Transduction Blaustein, M. Pelisch, F. Tanos, T. Muñoz, M.J. Wengier, D. Quadrana, L. Sanford, J.R. Muschietti, J.P. Kornblihtt, A.R. Cáceres, J.F. Coso, O.A. Srebrow, A. Concerted regulation of nuclear and cytoplasmic activities of SR proteins by AKT |
topic_facet |
fibronectin growth factor phosphatidylinositol 3 kinase protein protein kinase B serine arginine rich protein transfer RNA unclassified drug alternative RNA splicing article cytoplasm human nonhuman priority journal protein expression protein function protein localization RNA translation signal transduction 1-Phosphatidylinositol 3-Kinase Amino Acid Sequence Animals Cell Nucleus Cytoplasm Fibronectins Growth Substances Humans Molecular Sequence Data Nuclear Proteins Phosphoproteins Protein Biosynthesis Proto-Oncogene Proteins c-akt RNA Splicing RNA, Messenger RNA, Small Interfering RNA-Binding Proteins Signal Transduction |
description |
Serine/arginine-rich (SR) proteins are important regulators of mRNA splicing. Several postsplicing activities have been described for a subset of shuttling SR proteins, including regulation of mRNA export and translation. Using the fibronectin gene to study the links between signal-transduction pathways and SR protein activity, we show that growth factors not only modify the alternative splicing pattern of the fibronectin gene but also alter translation of reporter messenger RNAs in an SR protein-dependent fashion, providing two coregulated levels of isoform-specific amplification. These effects are inhibited by specific small interfering RNAs against SR proteins and are mediated by the AKT kinase, which elicits opposite effects to those evoked by overexpressing SR protein kinases CIk and SRPK. These results show how SR protein activity is modified in response to extracellular stimulation, leading to a concerted regulation of splicing and translation. © 2005 Nature Publishing Group. |
format |
JOUR |
author |
Blaustein, M. Pelisch, F. Tanos, T. Muñoz, M.J. Wengier, D. Quadrana, L. Sanford, J.R. Muschietti, J.P. Kornblihtt, A.R. Cáceres, J.F. Coso, O.A. Srebrow, A. |
author_facet |
Blaustein, M. Pelisch, F. Tanos, T. Muñoz, M.J. Wengier, D. Quadrana, L. Sanford, J.R. Muschietti, J.P. Kornblihtt, A.R. Cáceres, J.F. Coso, O.A. Srebrow, A. |
author_sort |
Blaustein, M. |
title |
Concerted regulation of nuclear and cytoplasmic activities of SR proteins by AKT |
title_short |
Concerted regulation of nuclear and cytoplasmic activities of SR proteins by AKT |
title_full |
Concerted regulation of nuclear and cytoplasmic activities of SR proteins by AKT |
title_fullStr |
Concerted regulation of nuclear and cytoplasmic activities of SR proteins by AKT |
title_full_unstemmed |
Concerted regulation of nuclear and cytoplasmic activities of SR proteins by AKT |
title_sort |
concerted regulation of nuclear and cytoplasmic activities of sr proteins by akt |
url |
http://hdl.handle.net/20.500.12110/paper_15459993_v12_n12_p1037_Blaustein |
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