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rdf:type |
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lifeskim:mentions |
umls-concept:C0162610,
umls-concept:C0243125,
umls-concept:C0662286,
umls-concept:C0699900,
umls-concept:C1514873,
umls-concept:C1521840,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1705165,
umls-concept:C2700061
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pubmed:issue |
11
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pubmed:dateCreated |
2003-6-3
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pubmed:abstractText |
SCF (Skp1-Cullin-F-box) complexes are a major class of E3 ligases that are required to selectively target substrates for ubiquitin-dependent degradation by the 26S proteasome. Conjugation of the ubiquitin-like protein Nedd8 to the cullin subunit (neddylation) positively regulates activity of SCF complexes, most likely by increasing their affinity for the E2 conjugated to ubiquitin. The Nedd8 conjugation pathway is required in C. elegans embryos for the ubiquitin-mediated degradation of the microtubule-severing protein MEI-1/Katanin at the meiosis-to-mitosis transition. Genetic experiments suggest that this pathway controls the activity of a CUL-3-based E3 ligase. Counteracting the Nedd8 pathway, the COP9/signalosome has been shown to promote deneddylation of the cullin subunit. However, little is known about the role of neddylation and deneddylation for E3 ligase activity in vivo.
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pubmed:grant |
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/COP9 signalosome complex,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cullin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MEI-1 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/katanin,
http://linkedlifedata.com/resource/pubmed/chemical/signalosome subunit 3
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0960-9822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
911-21
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12781129-Adenosine Triphosphatases,
pubmed-meshheading:12781129-Animals,
pubmed-meshheading:12781129-Caenorhabditis elegans,
pubmed-meshheading:12781129-Caenorhabditis elegans Proteins,
pubmed-meshheading:12781129-Cullin Proteins,
pubmed-meshheading:12781129-Immunoblotting,
pubmed-meshheading:12781129-Immunohistochemistry,
pubmed-meshheading:12781129-Meiosis,
pubmed-meshheading:12781129-Mitosis,
pubmed-meshheading:12781129-Multiprotein Complexes,
pubmed-meshheading:12781129-Nuclear Proteins,
pubmed-meshheading:12781129-Peptide Hydrolases,
pubmed-meshheading:12781129-Protein Kinases,
pubmed-meshheading:12781129-Proteins,
pubmed-meshheading:12781129-RNA Interference,
pubmed-meshheading:12781129-Two-Hybrid System Techniques,
pubmed-meshheading:12781129-Ubiquitins
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pubmed:year |
2003
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pubmed:articleTitle |
Neddylation and deneddylation of CUL-3 is required to target MEI-1/Katanin for degradation at the meiosis-to-mitosis transition in C. elegans.
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pubmed:affiliation |
Institute of Biochemistry, HPM G.10.1, ETH Hönggerberg, 8093 Zürich, Switzerland.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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