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Transportin-SR, a Nuclear Import Receptor for SR Proteins

The SR proteins, a group of abundant arginine/serine (RS)-rich proteins, are essential pre-mRNA splicing factors that are localized in the nucleus. The RS domain of these proteins serves as a nuclear localization signal. We found that RS domain–bearing proteins do not utilize any of the known nuclea...

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Detalles Bibliográficos
Autores principales: Kataoka, Naoyuki, Bachorik, Jennifer L., Dreyfuss, Gideon
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1999
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133142/
https://www.ncbi.nlm.nih.gov/pubmed/10366588
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author Kataoka, Naoyuki
Bachorik, Jennifer L.
Dreyfuss, Gideon
author_facet Kataoka, Naoyuki
Bachorik, Jennifer L.
Dreyfuss, Gideon
author_sort Kataoka, Naoyuki
collection PubMed
description The SR proteins, a group of abundant arginine/serine (RS)-rich proteins, are essential pre-mRNA splicing factors that are localized in the nucleus. The RS domain of these proteins serves as a nuclear localization signal. We found that RS domain–bearing proteins do not utilize any of the known nuclear import receptors and identified a novel nuclear import receptor specific for SR proteins. The SR protein import receptor, termed transportin-SR (TRN-SR), binds specifically and directly to the RS domains of ASF/SF2 and SC35 as well as several other SR proteins. The nuclear transport regulator RanGTP abolishes this interaction. Recombinant TRN-SR mediates nuclear import of RS domain– bearing proteins in vitro. TRN-SR has amino acid sequence similarity to several members of the importin β/transportin family. These findings strongly suggest that TRN-SR is a nuclear import receptor for the SR protein family.
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spelling pubmed-21331422008-05-01 Transportin-SR, a Nuclear Import Receptor for SR Proteins Kataoka, Naoyuki Bachorik, Jennifer L. Dreyfuss, Gideon J Cell Biol Article The SR proteins, a group of abundant arginine/serine (RS)-rich proteins, are essential pre-mRNA splicing factors that are localized in the nucleus. The RS domain of these proteins serves as a nuclear localization signal. We found that RS domain–bearing proteins do not utilize any of the known nuclear import receptors and identified a novel nuclear import receptor specific for SR proteins. The SR protein import receptor, termed transportin-SR (TRN-SR), binds specifically and directly to the RS domains of ASF/SF2 and SC35 as well as several other SR proteins. The nuclear transport regulator RanGTP abolishes this interaction. Recombinant TRN-SR mediates nuclear import of RS domain– bearing proteins in vitro. TRN-SR has amino acid sequence similarity to several members of the importin β/transportin family. These findings strongly suggest that TRN-SR is a nuclear import receptor for the SR protein family. The Rockefeller University Press 1999-06-14 /pmc/articles/PMC2133142/ /pubmed/10366588 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Kataoka, Naoyuki
Bachorik, Jennifer L.
Dreyfuss, Gideon
Transportin-SR, a Nuclear Import Receptor for SR Proteins
title Transportin-SR, a Nuclear Import Receptor for SR Proteins
title_full Transportin-SR, a Nuclear Import Receptor for SR Proteins
title_fullStr Transportin-SR, a Nuclear Import Receptor for SR Proteins
title_full_unstemmed Transportin-SR, a Nuclear Import Receptor for SR Proteins
title_short Transportin-SR, a Nuclear Import Receptor for SR Proteins
title_sort transportin-sr, a nuclear import receptor for sr proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133142/
https://www.ncbi.nlm.nih.gov/pubmed/10366588
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