rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2006-12-26
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pubmed:abstractText |
Cul5-based complex is a member of ECS (Elongin B/C-Cul2/Cul5-SOCS-box protein) ubiquitin ligase family. The cellular function of the Cul5-based complex is poorly understood. In this study, we found that oocyte septum formation and egg production did not occur in either cul-5- or rbx-2-depleted cul-2 homozygotes, although control cul-2 homozygotes laid approximately 50 eggs. These phenotypes are reminiscent of those caused by the MAP kinase mpk-1 depletion. In fact, activation of MPK-1 was significantly inhibited in cul-5-depleted cul-2 mutant and cul-2-depleted cul-5 mutant. Yeast two-hybrid analysis and RNAi-knockdown experiments suggest that oocyte maturation from pachytene exit and MPK-1 activation are redundantly controlled by the RBX-2-CUL-5- and RBX-1-CUL-2-based complexes.
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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/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cullin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/cullin-2 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/mpk-1 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
581
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
145-50
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17184777-Animals,
pubmed-meshheading:17184777-Animals, Genetically Modified,
pubmed-meshheading:17184777-Caenorhabditis elegans,
pubmed-meshheading:17184777-Caenorhabditis elegans Proteins,
pubmed-meshheading:17184777-Cullin Proteins,
pubmed-meshheading:17184777-Enzyme Activation,
pubmed-meshheading:17184777-Female,
pubmed-meshheading:17184777-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:17184777-Multiprotein Complexes,
pubmed-meshheading:17184777-Mutation,
pubmed-meshheading:17184777-Oocytes,
pubmed-meshheading:17184777-Oogenesis,
pubmed-meshheading:17184777-Ovoviviparity,
pubmed-meshheading:17184777-Pachytene Stage,
pubmed-meshheading:17184777-Protein-Serine-Threonine Kinases,
pubmed-meshheading:17184777-RNA, Small Interfering,
pubmed-meshheading:17184777-Ubiquitin-Protein Ligases
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pubmed:year |
2007
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pubmed:articleTitle |
C. elegans RBX-2-CUL-5- and RBX-1-CUL-2-based complexes are redundant for oogenesis and activation of the MAP kinase MPK-1.
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pubmed:affiliation |
Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba, Sendai, Miyagi, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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