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DEAD box protein DDX1 regulates cytoplasmic localization of KSRP

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 complexe...

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Published in:PloS one 2013-09, Vol.8 (9), p.e73752-e73752
Main Authors: Chou, Chu-Fang, Lin, Wei-Jye, Lin, Chen-Chung, Luber, Christian A, Godbout, Roseline, Mann, Matthias, Chen, Ching-Yi
Format: Article
Language:English
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0073752