Source:http://linkedlifedata.com/resource/pubmed/id/21146518
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2011-1-31
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pubmed:abstractText |
P granules, ribonucleoprotein (RNP) complexes specific to the cytoplasmic side of the nuclear pores of Caenorhabditis elegans germ cells, are implicated in post-transcriptional control of maternally-transcribed mRNAs. Here we show a relationship in C. elegans of Dicer, the riboendonuclease processing enzyme of the RNA interference and microRNA pathways, with GLH-1, a germline-specific RNA helicase and a constitutive component of P granules. Based on results from GST-pull-downs and immunoprecipitations, GLH-1 binds DCR-1 and this binding does not require RNA. Both GLH-1 protein and glh-1 mRNA levels are reduced in the dcr-1(ok247) null mutant background; conversely, a reduction of DCR-1 protein is observed in the glh-1(gk100) deletion strain. Thus, in the C. elegans germline, DCR-1 and GLH-1 are interdependent. In addition, evidence indicates that DCR-1 protein levels, like those of GLH-1, are likely regulated by the Jun N-terminal kinase (JNK), KGB-1. In adult germ cells, DCR-1 is found in uniformly-distributed, small puncta both throughout the cytoplasm and the nucleus, on the inner side of nuclear pores, and associated with P granules. In arrested oocytes, GLH-1 and DCR-1 re-localize to cytoplasmic and cortically-distributed RNP granules and are necessary to recruit other components to these complexes. We predict that the GLH-1/DCR-1 complex may function in the transport, deposition, or regulation of maternally-transcribed mRNAs and their associated miRNAs.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/GLH-1 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/KGB-1 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/MicroRNAs,
http://linkedlifedata.com/resource/pubmed/chemical/PGL-1 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease III,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/dcr-1 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1095-564X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
350
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
370-81
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pubmed:dateRevised |
2011-10-6
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pubmed:meshHeading |
pubmed-meshheading:21146518-Animals,
pubmed-meshheading:21146518-Caenorhabditis elegans,
pubmed-meshheading:21146518-Caenorhabditis elegans Proteins,
pubmed-meshheading:21146518-Cell Nucleus,
pubmed-meshheading:21146518-DEAD-box RNA Helicases,
pubmed-meshheading:21146518-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:21146518-MicroRNAs,
pubmed-meshheading:21146518-Nuclear Pore,
pubmed-meshheading:21146518-Oogenesis,
pubmed-meshheading:21146518-Protein Binding,
pubmed-meshheading:21146518-RNA Interference,
pubmed-meshheading:21146518-RNA-Binding Proteins,
pubmed-meshheading:21146518-Ribonuclease III,
pubmed-meshheading:21146518-Ribonucleoproteins
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pubmed:year |
2011
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pubmed:articleTitle |
C. elegans Dicer interacts with the P-granule component GLH-1 and both regulate germline RNPs.
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pubmed:affiliation |
Molecular Microbiology and Immunology Department, University of Missouri, Columbia, MO 65212, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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