rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2006-4-3
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pubmed:abstractText |
The mRNA processing body (P-body) is a cellular structure that has an important role in mRNA degradation. P-bodies have also been implicated in RNAi-mediated post-transcriptional gene silencing. The objective of this study was to identify and characterize novel components of the mammalian P-body. Approximately 5% of patients with the autoimmune disease primary biliary cirrhosis have antibodies directed against this structure. Serum from one of these patients was used to identify a cDNA encoding RAP55, a 463-amino acid protein. RAP55 colocalized with previously identified P-body components DCP1a and Ge-1. RAP55 contains an N-terminal Sm-like domain and two C-terminal RGG-rich domains separated by an FDF motif. The two RGG domains and the FDF domain were necessary and sufficient to target the protein to P-bodies. A fragment of RAP55 consisting of the FDF and the second RGG domains did not localize to P-bodies, but was able to displace other P-body components from this structure. After cells were subjected to arsenite-induced stress, RAP55 was detected in TIA-containing stress granules. The second RGG domain was necessary and sufficient for stress granule localization. siRNA-mediated knock-down of RAP55 resulted in loss of P-bodies, suggesting that RAP55 acts prior to the 5'-decapping step in mRNA degradation. The results of this study show that RAP55 is a component of P-bodies in cells at rest and localizes in stress granules in arsenite-treated cells. RAP55 may serve to shuttle mRNAs between P-bodies and stress granules.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-10747033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-11780629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-12440955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-12730603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-13130130,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-15257761,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-3047011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-6219389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-7520377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-8900092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16484376-9851867
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1355-8382
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
547-54
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16484376-Blotting, Western,
pubmed-meshheading:16484376-Cell Line,
pubmed-meshheading:16484376-Cytoplasmic Granules,
pubmed-meshheading:16484376-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:16484376-Humans,
pubmed-meshheading:16484376-Immunohistochemistry,
pubmed-meshheading:16484376-Protein Transport,
pubmed-meshheading:16484376-RNA, Messenger,
pubmed-meshheading:16484376-Ribonucleoproteins
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pubmed:year |
2006
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pubmed:articleTitle |
RNA-associated protein 55 (RAP55) localizes to mRNA processing bodies and stress granules.
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pubmed:affiliation |
Massachusetts General Hospital-East; CNY 8302, 149 13th Street, Charlestown, Massachusetts 02129, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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