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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
52
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pubmed:dateCreated |
2004-12-21
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pubmed:abstractText |
Expression of the intracellular tyrosine kinase BRK/Sik is epithelial-specific and regulated during differentiation. Only a few substrates have been identified for BRK/Sik, including the KH domain containing RNA-binding protein Sam68 and the novel adaptor protein BKS. Although the physiological role of Sam68 is unknown, it has been shown to regulate mRNA transport, pre-mRNA splicing, and polyadenylation. Here we demonstrate that the Sam68-like mammalian proteins SLM-1 and SLM-2 but not the related KH domain containing heterogeneous nuclear ribonucleoprotein K are novel substrates of BRK/Sik. The expression of active BRK/Sik results in increased SLM-1 and SLM-2 phosphorylation and increased retention of BRK/Sik within the nucleus. The phosphorylation of SLM-1 and SLM-2 has functional relevance and leads to inhibition of their RNA-binding abilities. We show that SLM-1, SLM-2, and BRK/Sik have restricted patterns of expression unlike the ubiquitously expressed Sam68. Moreover, BRK/Sik, SLM-1, and Sam68 transcripts were coexpressed in the mouse gastrointestinal tract and skin, suggesting that SLM-1 and Sam68 could be physiologically relevant BRK/Sik targets in vivo. The ability of BRK/Sik to negatively regulate the RNA-binding activities of the KH domain RNA binding proteins SLM-1 and Sam68 may have an impact on the posttranscriptional regulation of epithelial cell gene expression.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/KHDRBS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Khdrbs1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Khdrbs2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Khdrbs3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PTK6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/green fluorescent protein...,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/src-related intestinal kinase, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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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 |
24
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
54398-404
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pubmed:dateRevised |
2010-12-7
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pubmed:meshHeading |
pubmed-meshheading:15471878-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:15471878-Animals,
pubmed-meshheading:15471878-Cell Line,
pubmed-meshheading:15471878-Cell Nucleus,
pubmed-meshheading:15471878-DNA-Binding Proteins,
pubmed-meshheading:15471878-Epithelium,
pubmed-meshheading:15471878-Female,
pubmed-meshheading:15471878-Gastrointestinal Tract,
pubmed-meshheading:15471878-Gene Expression,
pubmed-meshheading:15471878-Green Fluorescent Proteins,
pubmed-meshheading:15471878-HeLa Cells,
pubmed-meshheading:15471878-Humans,
pubmed-meshheading:15471878-Male,
pubmed-meshheading:15471878-Mammary Glands, Animal,
pubmed-meshheading:15471878-Mice,
pubmed-meshheading:15471878-Neoplasm Proteins,
pubmed-meshheading:15471878-Phosphorylation,
pubmed-meshheading:15471878-Protein-Tyrosine Kinases,
pubmed-meshheading:15471878-RNA,
pubmed-meshheading:15471878-RNA, Messenger,
pubmed-meshheading:15471878-RNA-Binding Proteins,
pubmed-meshheading:15471878-Recombinant Fusion Proteins,
pubmed-meshheading:15471878-Skin,
pubmed-meshheading:15471878-Substrate Specificity,
pubmed-meshheading:15471878-Testis,
pubmed-meshheading:15471878-Transfection,
pubmed-meshheading:15471878-Tyrosine,
pubmed-meshheading:15471878-src-Family Kinases
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pubmed:year |
2004
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pubmed:articleTitle |
The nuclear tyrosine kinase BRK/Sik phosphorylates and inhibits the RNA-binding activities of the Sam68-like mammalian proteins SLM-1 and SLM-2.
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pubmed:affiliation |
Departments of Biochemistry and Molecular Genetics, University of Illinois, Chicago, Illinois 60607, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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