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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
35
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pubmed:dateCreated |
2003-8-25
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pubmed:abstractText |
Messenger RNA turnover directed by A + U-rich elements (AREs) involves selected ARE-binding proteins. Whereas several signaling systems may modulate ARE-directed mRNA decay and/or post-translationally modify specific trans-acting factors, it is unclear how these mechanisms are linked. In THP-1 monocytic leukemia cells, phorbol ester-induced stabilization of some mRNAs containing AREs was accompanied by dephosphorylation of Ser83 and Ser87 of polysome-associated p40AUF1. Here, we report that phosphorylation of p40AUF1 influences its ARE-binding affinity as well as the RNA conformational dynamics and global structure of the p40AUF1-ARE ribonucleoprotein complex. Most notably, association of unphosphorylated p40AUF1 induces a condensed RNA conformation upon ARE substrates. By contrast, phosphorylation of p40AUF1 at Ser83 and Ser87 inhibits this RNA structural transition. These data indicate that selective AUF1 phosphorylation may regulate ARE-directed mRNA turnover by remodeling local RNA structures, thus potentially altering the presentation of RNA and/or protein determinants involved in subsequent trans-factor recruitment.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Heterogeneous-Nuclear...,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/glycogen synthase kinase 3 beta,
http://linkedlifedata.com/resource/pubmed/chemical/hnRNP D0
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33039-48
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:12819194-Amino Acid Sequence,
pubmed-meshheading:12819194-Anisotropy,
pubmed-meshheading:12819194-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:12819194-Dimerization,
pubmed-meshheading:12819194-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:12819194-Glycogen Synthase Kinase 3,
pubmed-meshheading:12819194-Heterogeneous-Nuclear Ribonucleoprotein D,
pubmed-meshheading:12819194-Histidine,
pubmed-meshheading:12819194-Humans,
pubmed-meshheading:12819194-Kinetics,
pubmed-meshheading:12819194-Models, Chemical,
pubmed-meshheading:12819194-Models, Statistical,
pubmed-meshheading:12819194-Molecular Sequence Data,
pubmed-meshheading:12819194-Nucleic Acid Conformation,
pubmed-meshheading:12819194-Oligonucleotides,
pubmed-meshheading:12819194-Phosphorylation,
pubmed-meshheading:12819194-Protein Binding,
pubmed-meshheading:12819194-Protein Conformation,
pubmed-meshheading:12819194-Protein Processing, Post-Translational,
pubmed-meshheading:12819194-Protein Structure, Tertiary,
pubmed-meshheading:12819194-RNA,
pubmed-meshheading:12819194-RNA, Messenger,
pubmed-meshheading:12819194-Recombinant Proteins,
pubmed-meshheading:12819194-Ribonucleoproteins,
pubmed-meshheading:12819194-Serine,
pubmed-meshheading:12819194-Signal Transduction,
pubmed-meshheading:12819194-Spectrometry, Fluorescence,
pubmed-meshheading:12819194-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:12819194-Thermodynamics,
pubmed-meshheading:12819194-Time Factors,
pubmed-meshheading:12819194-Tumor Cells, Cultured
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pubmed:year |
2003
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pubmed:articleTitle |
Phosphorylation of p40AUF1 regulates binding to A + U-rich mRNA-destabilizing elements and protein-induced changes in ribonucleoprotein structure.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology and Center for Fluorescence Spectroscopy, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA. gwils001@umaryland.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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