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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2010-1-27
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pubmed:abstractText |
The abundant heterogeneous nuclear ribonucleoprotein M (hnRNP M) is able to associate with early spliceosomes and to influence splicing patterns of specific pre-mRNAs. Here, by a combination of immunoprecipitation and pull-down assays, we have identified PSF (polypyrimidine tract-binding protein-associated splicing factor) and p54(nrb), two highly related proteins involved in transcription and RNA processing, as new binding partners of hnRNP M. HnRNP M was found to co-localize with PSF within a subset of nuclear paraspeckles and to largely co-fractionate with PSF and p54(nrb) in biochemical nuclear matrix preparations. In cells transfected with an alternatively spliced preprotachykinin (PPT) minigene expression of hnRNP M promoted exon skipping while expression of PSF favours exon inclusion. The latter effect was reverted specifically by co-expressing the full length hnRNP M or a deletion mutant capable of interaction with PSF and p54(nrb). Together our data provide new insights and some functional implications on the hnRNP M network of interactions.
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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/Cell Extracts,
http://linkedlifedata.com/resource/pubmed/chemical/Heterogeneous-Nuclear...,
http://linkedlifedata.com/resource/pubmed/chemical/NONO protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Matrix-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Octamer Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/PTB-associated splicing factor,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tachykinins,
http://linkedlifedata.com/resource/pubmed/chemical/preprotachykinin
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1090-2422
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2009 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
316
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
390-400
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pubmed:meshHeading |
pubmed-meshheading:19874820-Alternative Splicing,
pubmed-meshheading:19874820-Cell Extracts,
pubmed-meshheading:19874820-Cell Fractionation,
pubmed-meshheading:19874820-Cell Nucleus Structures,
pubmed-meshheading:19874820-Exons,
pubmed-meshheading:19874820-Heterogeneous-Nuclear Ribonucleoprotein Group M,
pubmed-meshheading:19874820-Humans,
pubmed-meshheading:19874820-Nuclear Matrix,
pubmed-meshheading:19874820-Nuclear Matrix-Associated Proteins,
pubmed-meshheading:19874820-Octamer Transcription Factors,
pubmed-meshheading:19874820-Protein Binding,
pubmed-meshheading:19874820-Protein Precursors,
pubmed-meshheading:19874820-RNA-Binding Proteins,
pubmed-meshheading:19874820-Recombinant Proteins,
pubmed-meshheading:19874820-Tachykinins
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pubmed:year |
2010
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pubmed:articleTitle |
hnRNP M interacts with PSF and p54(nrb) and co-localizes within defined nuclear structures.
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pubmed:affiliation |
RNA Processing Laboratory, Institute of Biological Research and Biotechnology, National Hellenic Research Foundation, 48 Vas. Constantinou Avenue, 11635 Athens, Greece.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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