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  DEAD Box Protein DDX1 Regulates Cytoplasmic Localization of KSRP

Chou, C.-F., Lin, W.-J., Lin, C.-C., Luber, C. A., Godbout, R., Mann, M., et al. (2013). DEAD Box Protein DDX1 Regulates Cytoplasmic Localization of KSRP. PLOS ONE, 8(9): e73752. doi:10.1371/journal.pone.0073752.

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 Urheber:
Chou, Chu-Fang1, Autor
Lin, Wei-Jye1, Autor
Lin, Chen-Chung1, Autor
Luber, Christian A.2, Autor           
Godbout, Roseline1, Autor
Mann, Matthias2, Autor           
Chen, Ching-Yi1, Autor
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Schlagwörter: AU-RICH ELEMENT; MESSENGER-RNA TURNOVER; ZINC-FINGER PROTEINS; BINDING-PROTEIN; GENE-EXPRESSION; HNRNP D; HUR; DEGRADATION; DECAY; TRISTETRAPROLIN
 Zusammenfassung: mRNA decay mediated by the AU-rich elements (AREs) is one of the most studied post-transcriptional mechanisms and is modulated by ARE-binding proteins (ARE-BPs). To understand the regulation of K homology splicing regulatory protein (KSRP), a decay-promoting ARE-BP, we purified KSRP protein complexes and identified an RNA helicase, DDX1. We showed that down-regulation of DDX1 expression elevated cytoplasmic levels of KSRP and facilitated ARE-mediated mRNA decay. Association of KSRP with 14-3-3 proteins, that are predominately located in the cytoplasm, increased upon reduction of DDX1. We also demonstrated that KSRP associated with DDX1 or 14-3-3, but not both. These observations indicate that subcellular localization of KSRP is regulated by competing interactions with DDX1 or 14-3-3.

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Sprache(n): eng - English
 Datum: 2013
 Publikationsstatus: Online veröffentlicht
 Seiten: 8
 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000324515600116
DOI: 10.1371/journal.pone.0073752
 Art des Abschluß: -

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Titel: PLOS ONE
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA : PUBLIC LIBRARY SCIENCE
Seiten: - Band / Heft: 8 (9) Artikelnummer: e73752 Start- / Endseite: - Identifikator: ISSN: 1932-6203