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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2005-6-3
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pubmed:abstractText |
The Nova family of neuron-specific RNA-binding proteins were originally identified as targets in an autoimmune neurologic disease characterized by failure of motor inhibition. Nova-1 regulates alternative splicing of pre-mRNAs encoding the inhibitory neurotransmitter receptor subunits GABA(A)Rgamma2 and GlyRalpha2 by directly binding intronic elements, resulting in enhancement of exon inclusion. Here we identify exon E4 in the Nova-1 pre-mRNA itself, encoding a phosphorylated protein domain, as an additional target of Nova-dependent splicing regulation in the mouse spinal cord. Nova binding to E4 is necessary and sufficient for Nova-dependent exon exclusion. E4 harbors five repeats of the known Nova-binding tetranucleotide YCAY and mutation of these elements destroys Nova-dependent regulation. Furthermore, swapping of the sites from Nova-1 and GABA(A)Rgamma2 indicates that the ability of Nova to enhance or repress alternative exon inclusion is dependent on the position of the Nova-binding element within the pre-mRNA. These studies demonstrate that in addition to its previously described role as a splicing activator, Nova autoregulates its own expression by acting as a splicing repressor.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-10202157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-10490636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-10676814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-11779509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-11967553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-12114529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-12202761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-12600273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-12626338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-12808107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-12824367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-14561798,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-14615540,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-14684825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-1531115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-2015625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-2063196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-2238044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-2820993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-8398153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-8558240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-8632829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-8755249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-8825483,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-9154818,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-9603524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15933722-9789075
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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/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/GLRA2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glra2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nova antigen,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, GABA-A,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glycine
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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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 |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1608-20
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15933722-Alternative Splicing,
pubmed-meshheading:15933722-Amino Acid Sequence,
pubmed-meshheading:15933722-Animals,
pubmed-meshheading:15933722-Antigens, Neoplasm,
pubmed-meshheading:15933722-Base Sequence,
pubmed-meshheading:15933722-Binding Sites,
pubmed-meshheading:15933722-Cell Line,
pubmed-meshheading:15933722-Exons,
pubmed-meshheading:15933722-Gene Expression Regulation,
pubmed-meshheading:15933722-Humans,
pubmed-meshheading:15933722-Mice,
pubmed-meshheading:15933722-Molecular Sequence Data,
pubmed-meshheading:15933722-Nerve Tissue Proteins,
pubmed-meshheading:15933722-Neurons,
pubmed-meshheading:15933722-Protein Structure, Tertiary,
pubmed-meshheading:15933722-RNA Precursors,
pubmed-meshheading:15933722-RNA-Binding Proteins,
pubmed-meshheading:15933722-Receptors, GABA-A,
pubmed-meshheading:15933722-Receptors, Glycine,
pubmed-meshheading:15933722-Sequence Alignment
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pubmed:year |
2005
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pubmed:articleTitle |
Nova autoregulation reveals dual functions in neuronal splicing.
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pubmed:affiliation |
Laboratory of Molecular Neuro-Oncology, Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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