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DEAD Box Protein DDX1 Regulates Cytoplasmic Localization of KSRP

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78339

Luber,  Christian A.
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78356

Mann,  Matthias
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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journal.pone.0073752.pdf
(beliebiger Volltext), 2MB

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Zitation

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.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-7849-6
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.