Source:http://linkedlifedata.com/resource/pubmed/id/19122807
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
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| pubmed:dateCreated |
2011-9-23
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| pubmed:abstractText |
Previous studies using the yeast two-hybrid assay (Y2H) have identified cyclin L1 (CCNL1) and Ewing sarcoma breakpoint region 1 protein (EWSR1) as being interacting partners of tuftelin-interacting protein 11 (TFIP11). All three proteins are functionally related to the spliceosome and involved in pre-mRNA splicing activities. The spliceosome is a dynamic ribonucleoprotein complex responsible for pre-mRNA splicing of intronic regions, and is composed of five small nuclear RNAs (snRNAs) and ?140 proteins. TFIP11 appears to play a role in spliceosome disassembly allowing for the release of the bound lariat-intron. The roles of CCNL1 and EWSR1 in the spliceosome are poorly understood. Using fluorescently-tagged proteins and confocal microscopy we show that TFIP11, CCNL1 and EWSR1 frequently co-localize to speckled nuclear domains. These data would suggest that all three proteins participate in a common cellular activity related to RNA splicing events.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Aug
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| pubmed:issn |
1422-0067
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
9
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1504-14
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| pubmed:year |
2008
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| pubmed:articleTitle |
TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization.
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| pubmed:affiliation |
University of Southern California, School of Dentistry, Center for Craniofacial Molecular Biology, 2250 Alcazar Street, CSA room 103, Los Angeles, California 90033-1004, USA. E-mail: paine@usc.edu.
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| pubmed:publicationType |
Journal Article
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