Source:http://linkedlifedata.com/resource/pubmed/id/15466891
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 22
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| pubmed:dateCreated |
2004-10-14
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| pubmed:abstractText |
The anaphase-promoting complex or cyclosome (APC/C) is a multi-subunit ubiquitin ligase that regulates the eukaryotic cell cycle. APC/C belongs to the RING finger class of ubiquitin ligases that function by interacting with a ubiquitin-conjugating enzyme (Ubc), thus inciting the Ubc to transfer ubiquitin onto a target protein. Extensive studies with APC/C in other organisms have identified several possible Ubcs that might function as partners for APC/C. This report presents phenotypic and biochemical evidence showing that, in Caenorhabditis elegans, UBC-2 interacts specifically with the APC/C. This conclusion is based on three lines of evidence: first, the RNAi phenotype of ubc-2 is indistinguishable from RNAi phenotypes of APC/C subunits; second, RNAi of ubc-2 but not other Ubcs enhances the phenotype of hypomorphic APC/C mutants; third, purified UBC-2 and APC-11, the RING finger subunit of the APC/C, show robust ubiquitination activity in in vitro assays. APC-11 interaction is specific for UBC-2 as ubiquitination is not seen when APC-11 is combined other C. elegans Ubcs. As expected from the Ubc that functions with the APC/C, ubc-2(RNAi) produces metaphase blocks in both mitotic germ cells and in meiotic divisions of post-fertilization oocytes. In addition, ubc-2(RNAi) results in two germline phenotypes that appear to be unrelated to the APC/C: an expanded transition zone indicative of a pre-pachytene meiotic arrest and endo-reduplicated oocytes indicative of a problem in ovulation or oocyte-soma interactions.
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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/Ubiquitin-Conjugating Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligase Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/anaphase-promoting complex,
http://linkedlifedata.com/resource/pubmed/chemical/let-70 protein, C elegans
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0021-9533
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
117
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
5427-35
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:15466891-Alleles,
pubmed-meshheading:15466891-Amino Acid Sequence,
pubmed-meshheading:15466891-Anaphase,
pubmed-meshheading:15466891-Animals,
pubmed-meshheading:15466891-Caenorhabditis elegans,
pubmed-meshheading:15466891-Caenorhabditis elegans Proteins,
pubmed-meshheading:15466891-Meiosis,
pubmed-meshheading:15466891-Metaphase,
pubmed-meshheading:15466891-Microscopy, Fluorescence,
pubmed-meshheading:15466891-Mitosis,
pubmed-meshheading:15466891-Molecular Sequence Data,
pubmed-meshheading:15466891-Mutation,
pubmed-meshheading:15466891-Oocytes,
pubmed-meshheading:15466891-Phenotype,
pubmed-meshheading:15466891-Plasmids,
pubmed-meshheading:15466891-RNA Interference,
pubmed-meshheading:15466891-Ubiquitin-Conjugating Enzymes,
pubmed-meshheading:15466891-Ubiquitin-Protein Ligase Complexes,
pubmed-meshheading:15466891-Ubiquitin-Protein Ligases
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| pubmed:year |
2004
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| pubmed:articleTitle |
Caenorhabditis elegans UBC-2 functions with the anaphase-promoting complex but also has other activities.
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| pubmed:affiliation |
Department of Biological Sciences, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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