DEAD box protein DDX1 regulates cytoplasmic localization of KSRP

Chu-Fang Chou; Wei-Jye Lin; Chen-Chung Lin; Christian A Luber; Roseline Godbout; Matthias Mann; Ching-Yi Chen

doi:10.1371/journal.pone.0073752

DEAD box protein DDX1 regulates cytoplasmic localization of KSRP

Chu-Fang Chou, Wei-Jye Lin, Chen-Chung Lin, Christian A Luber, Roseline Godbout, Matthias Mann, Ching-Yi Chen

7 Citations (Scopus)

Abstract

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.

Original language	English
Article number	e73752
Journal	P L o S One
Volume	8
Issue number	9
ISSN	1932-6203
DOIs	https://doi.org/10.1371/journal.pone.0073752
Publication status	Published - 4 Sept 2013
Externally published	Yes

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title = "DEAD box protein DDX1 regulates cytoplasmic localization of KSRP",

abstract = "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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doi = "10.1371/journal.pone.0073752",

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T1 - DEAD box protein DDX1 regulates cytoplasmic localization of KSRP

AU - Chou, Chu-Fang

AU - Lin, Wei-Jye

AU - Lin, Chen-Chung

AU - Luber, Christian A

AU - Godbout, Roseline

AU - Mann, Matthias

AU - Chen, Ching-Yi

PY - 2013/9/4

Y1 - 2013/9/4

N2 - 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.

AB - 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.

U2 - 10.1371/journal.pone.0073752

DO - 10.1371/journal.pone.0073752

M3 - Journal article

C2 - 24023901

SN - 1932-6203

VL - 8

JO - PLoS Computational Biology

JF - PLoS Computational Biology

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DEAD box protein DDX1 regulates cytoplasmic localization of KSRP

Abstract

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