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A family of RS domain proteins with novel subcellular localization and trafficking
We report the sequence, conservation and cell biology of a novel protein, Psc1, which is expressed and regulated within the embryonic pluripotent cell population of the mouse. The Psc1 sequence includes an RS domain and an RNA recognition motif (RRM), and a sequential arrangement of protein motifs t...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC552957/ https://www.ncbi.nlm.nih.gov/pubmed/15741184 http://dx.doi.org/10.1093/nar/gki269 |
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author | Kavanagh, Steven J. Schulz, Thomas C. Davey, Philippa Claudianos, Charles Russell, Carrie Rathjen, Peter D. |
author_facet | Kavanagh, Steven J. Schulz, Thomas C. Davey, Philippa Claudianos, Charles Russell, Carrie Rathjen, Peter D. |
author_sort | Kavanagh, Steven J. |
collection | PubMed |
description | We report the sequence, conservation and cell biology of a novel protein, Psc1, which is expressed and regulated within the embryonic pluripotent cell population of the mouse. The Psc1 sequence includes an RS domain and an RNA recognition motif (RRM), and a sequential arrangement of protein motifs that has not been demonstrated for other RS domain proteins. This arrangement was conserved in a second mouse protein (BAC34721). The identification of Psc1 and BAC34721 homologues in vertebrates and related proteins, more widely throughout evolution, defines a new family of RS domain proteins termed acidic rich RS (ARRS) domain proteins. Psc1 incorporated into the nuclear speckles, but demonstrated novel aspects of subcellular distribution including localization to speckles proximal to the nuclear periphery and localization to punctate structures in the cytoplasm termed cytospeckles. Integration of Psc1 into cytospeckles was dependent on the RRM. Cytospeckles were dynamic within the cytoplasm and appeared to traffic into the nucleus. These observations suggest a novel role in RNA metabolism for ARRS proteins. |
format | Text |
id | pubmed-552957 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-5529572005-03-10 A family of RS domain proteins with novel subcellular localization and trafficking Kavanagh, Steven J. Schulz, Thomas C. Davey, Philippa Claudianos, Charles Russell, Carrie Rathjen, Peter D. Nucleic Acids Res Article We report the sequence, conservation and cell biology of a novel protein, Psc1, which is expressed and regulated within the embryonic pluripotent cell population of the mouse. The Psc1 sequence includes an RS domain and an RNA recognition motif (RRM), and a sequential arrangement of protein motifs that has not been demonstrated for other RS domain proteins. This arrangement was conserved in a second mouse protein (BAC34721). The identification of Psc1 and BAC34721 homologues in vertebrates and related proteins, more widely throughout evolution, defines a new family of RS domain proteins termed acidic rich RS (ARRS) domain proteins. Psc1 incorporated into the nuclear speckles, but demonstrated novel aspects of subcellular distribution including localization to speckles proximal to the nuclear periphery and localization to punctate structures in the cytoplasm termed cytospeckles. Integration of Psc1 into cytospeckles was dependent on the RRM. Cytospeckles were dynamic within the cytoplasm and appeared to traffic into the nucleus. These observations suggest a novel role in RNA metabolism for ARRS proteins. Oxford University Press 2005 2005-03-01 /pmc/articles/PMC552957/ /pubmed/15741184 http://dx.doi.org/10.1093/nar/gki269 Text en © The Author 2005. Published by Oxford University Press. All rights reserved |
spellingShingle | Article Kavanagh, Steven J. Schulz, Thomas C. Davey, Philippa Claudianos, Charles Russell, Carrie Rathjen, Peter D. A family of RS domain proteins with novel subcellular localization and trafficking |
title | A family of RS domain proteins with novel subcellular localization and trafficking |
title_full | A family of RS domain proteins with novel subcellular localization and trafficking |
title_fullStr | A family of RS domain proteins with novel subcellular localization and trafficking |
title_full_unstemmed | A family of RS domain proteins with novel subcellular localization and trafficking |
title_short | A family of RS domain proteins with novel subcellular localization and trafficking |
title_sort | family of rs domain proteins with novel subcellular localization and trafficking |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC552957/ https://www.ncbi.nlm.nih.gov/pubmed/15741184 http://dx.doi.org/10.1093/nar/gki269 |
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