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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
2006-9-21
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pubmed:abstractText |
In myotonic dystrophy (DM1), both inactivation of muscleblind proteins and increased levels of CUG-BP1 are reported. These events have been shown to contribute independently to aberrant splicing of a subset RNAs. We demonstrate that steady-state levels of the splice regulator, hnRNP H, are elevated in DM1 myoblasts and that increased hnRNP H levels in normal myoblasts results in the inhibition of insulin receptor (IR) exon 11 splicing in a manner similar to that observed in DM1. In normal myoblasts, overexpression of either hnRNP H or CUG-BP1 results in the formation of an RNA-dependent suppressor complex consisting of both hnRNP H and CUG-BP1, which is required to maximally inhibit IR exon 11 inclusion. Elevated levels of MBNL1 show RNA-independent interaction with hnRNP H and dampen the inhibitory activity of increased hnRNP H levels on IR splicing in normal myoblasts. In DM1 myoblasts, overexpression of MBNL1 in conjunction with si-RNA mediated depletion of hnRNP H contributes to partial rescue of the IR splicing defect. These data demonstrate that coordinated physical and functional interactions between hnRNP H, CUG-BP1 and MBNL1 dictate IR splicing in normal and DM1 myoblasts.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-10970838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-10976074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-11124939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-11158314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-11486088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-11528389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-11726559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-11929853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-12150905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-12150906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-12217958,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-1310900,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-14671308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-15257297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-1546325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-1546326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-15496431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-15546872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-15843400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-15972723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-16027111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-2538124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-7896884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-8469976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-8595416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-8948631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-9241282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-9241283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-9553088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16946708-9563950
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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/CELF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Heterogeneous-Nuclear...,
http://linkedlifedata.com/resource/pubmed/chemical/MBNL1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/myotonic dystrophy protein kinase
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4271-83
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pubmed:dateRevised |
2010-9-16
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pubmed:meshHeading |
pubmed-meshheading:16946708-Base Sequence,
pubmed-meshheading:16946708-Cells, Cultured,
pubmed-meshheading:16946708-Heterogeneous-Nuclear Ribonucleoprotein Group F-H,
pubmed-meshheading:16946708-Humans,
pubmed-meshheading:16946708-Models, Biological,
pubmed-meshheading:16946708-Multiprotein Complexes,
pubmed-meshheading:16946708-Myoblasts,
pubmed-meshheading:16946708-Myotonic Dystrophy,
pubmed-meshheading:16946708-Protein-Serine-Threonine Kinases,
pubmed-meshheading:16946708-RNA, Small Interfering,
pubmed-meshheading:16946708-RNA Splicing,
pubmed-meshheading:16946708-RNA-Binding Proteins,
pubmed-meshheading:16946708-Receptor, Insulin,
pubmed-meshheading:16946708-Recombinant Proteins,
pubmed-meshheading:16946708-Transfection
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pubmed:year |
2006
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pubmed:articleTitle |
Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-associated aberrant IR splicing.
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pubmed:affiliation |
Institute for Genetic Medicine, Keck School of Medicine, University of Southern California, Los Angeles, CA 90033, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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