DEAD box protein DDX1 regulates cytoplasmic localization of KSRP

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DEAD box protein DDX1 regulates cytoplasmic localization of KSRP. / Chou, Chu-Fang; Lin, Wei-Jye; Lin, Chen-Chung; Luber, Christian A; Godbout, Roseline; Mann, Matthias; Chen, Ching-Yi.

I: P L o S One, Bind 8, Nr. 9, e73752, 04.09.2013.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning

Harvard

Chou, C-F, Lin, W-J, Lin, C-C, Luber, CA, Godbout, R, Mann, M & Chen, C-Y 2013, 'DEAD box protein DDX1 regulates cytoplasmic localization of KSRP', P L o S One, bind 8, nr. 9, e73752. https://doi.org/10.1371/journal.pone.0073752

APA

Chou, C-F., Lin, W-J., Lin, C-C., Luber, C. A., Godbout, R., Mann, M., & Chen, C-Y. (2013). DEAD box protein DDX1 regulates cytoplasmic localization of KSRP. P L o S One, 8(9), [e73752]. https://doi.org/10.1371/journal.pone.0073752

Vancouver

Chou C-F, Lin W-J, Lin C-C, Luber CA, Godbout R, Mann M o.a. DEAD box protein DDX1 regulates cytoplasmic localization of KSRP. P L o S One. 2013 sep. 4;8(9). e73752. https://doi.org/10.1371/journal.pone.0073752

Author

Chou, Chu-Fang ; Lin, Wei-Jye ; Lin, Chen-Chung ; Luber, Christian A ; Godbout, Roseline ; Mann, Matthias ; Chen, Ching-Yi. / DEAD box protein DDX1 regulates cytoplasmic localization of KSRP. I: P L o S One. 2013 ; Bind 8, Nr. 9.

Bibtex

@article{eca4b96ca43e4603a97d9616268ceace,

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.",

author = "Chu-Fang Chou and Wei-Jye Lin and Chen-Chung Lin and Luber, {Christian A} and Roseline Godbout and Matthias Mann and Ching-Yi Chen",

year = "2013",

month = sep,

day = "4",

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

language = "English",

volume = "8",

journal = "PLoS ONE",

issn = "1932-6203",

publisher = "Public Library of Science",

number = "9",

}

RIS

TY - JOUR

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

VL - 8

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 9

M1 - e73752

ER -

ID: 88188566