rdf:type |
|
lifeskim:mentions |
umls-concept:C0013879,
umls-concept:C0208973,
umls-concept:C0439851,
umls-concept:C0598720,
umls-concept:C0699789,
umls-concept:C1145667,
umls-concept:C1417898,
umls-concept:C1423088,
umls-concept:C1517892,
umls-concept:C1552596,
umls-concept:C1704259,
umls-concept:C1704666,
umls-concept:C1705987,
umls-concept:C1947931,
umls-concept:C1999230
|
pubmed:issue |
48
|
pubmed:dateCreated |
2006-11-27
|
pubmed:abstractText |
Retroviruses/retroelements provide tools enabling the identification and dissection of basic steps for post-transcriptional regulation of cellular mRNAs. The RNA transport element (RTE) identified in mouse retrotransposons is functionally equivalent to constitutive transport element of Type D retroviruses, yet does not bind directly to the mRNA export receptor NXF1. Here, we report that the RNA-binding motif protein 15 (RBM15) recognizes RTE directly and specifically in vitro and stimulates export and expression of RTE-containing reporter mRNAs in vivo. Tethering of RBM15 to a reporter mRNA showed that RBM15 acts by promoting mRNA export from the nucleus. We also found that RBM15 binds to NXF1 and the two proteins cooperate in stimulating RTE-mediated mRNA export and expression. Thus, RBM15 is a novel mRNA export factor and is part of the NXF1 pathway. We propose that RTE evolved as a high affinity RBM15 ligand to provide a splicing-independent link to NXF1, thereby ensuring efficient nuclear export and expression of retrotransposon transcripts.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
281
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
36915-28
|
pubmed:meshHeading |
pubmed-meshheading:17001072-Alternative Splicing,
pubmed-meshheading:17001072-Amino Acid Motifs,
pubmed-meshheading:17001072-Amino Acid Sequence,
pubmed-meshheading:17001072-Animals,
pubmed-meshheading:17001072-Base Sequence,
pubmed-meshheading:17001072-HeLa Cells,
pubmed-meshheading:17001072-Humans,
pubmed-meshheading:17001072-Ligands,
pubmed-meshheading:17001072-Mice,
pubmed-meshheading:17001072-Models, Biological,
pubmed-meshheading:17001072-Molecular Sequence Data,
pubmed-meshheading:17001072-Nucleocytoplasmic Transport Proteins,
pubmed-meshheading:17001072-RNA,
pubmed-meshheading:17001072-RNA, Messenger,
pubmed-meshheading:17001072-RNA-Binding Proteins,
pubmed-meshheading:17001072-Retroviridae
|
pubmed:year |
2006
|
pubmed:articleTitle |
RNA-binding motif protein 15 binds to the RNA transport element RTE and provides a direct link to the NXF1 export pathway.
|
pubmed:affiliation |
Human Retrovirus Section.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|