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rdf:type |
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lifeskim:mentions |
umls-concept:C0086418,
umls-concept:C0105770,
umls-concept:C0243125,
umls-concept:C0265264,
umls-concept:C0376315,
umls-concept:C0699900,
umls-concept:C1166721,
umls-concept:C1334043,
umls-concept:C1420081,
umls-concept:C1521840,
umls-concept:C1539505
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pubmed:issue |
12
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pubmed:dateCreated |
1999-6-3
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pubmed:databankReference |
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pubmed:abstractText |
SCF E3 ubiquitin ligases mediate ubiquitination and proteasome-dependent degradation of phosphorylated substrates. We identified a human F-box/WD40 repeats protein (HOS), which is homologous to Slimb/h betaTrCP. Being a part of SCF complex with Skp1 and Cullin1, HOS specifically interacted with the phosphorylated IkappaB and beta-catenin, targeting these proteins for proteasome-dependent degradation in vivo. This targeting required Cullin1 as expression of a mutant Cullin1 abrogated the degradation of IkappaB and of beta-catenin. Mutant HOS which lacks the F-box blocked TNF alpha-induced degradation of IkappaB as well as GSK3beta-mediated degradation of beta-catenin. This mutant also inhibited NF-kappaB transactivation and increased the beta-catenin-dependent transcription activity of Tcf. These results demonstrate that SCF(HOS) E3 ubiquitin ligase regulate both NF-kappaB and beta-catenin signaling pathways.
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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/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FBXW11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/SKP Cullin F-Box Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Transducin Repeat-Containing...,
http://linkedlifedata.com/resource/pubmed/chemical/supernumerary limbs protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0950-9232
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2039-46
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10321728-Amino Acid Sequence,
pubmed-meshheading:10321728-Carrier Proteins,
pubmed-meshheading:10321728-Cell Cycle Proteins,
pubmed-meshheading:10321728-Cytoskeletal Proteins,
pubmed-meshheading:10321728-DNA-Binding Proteins,
pubmed-meshheading:10321728-Drosophila Proteins,
pubmed-meshheading:10321728-Humans,
pubmed-meshheading:10321728-Insect Proteins,
pubmed-meshheading:10321728-Ligases,
pubmed-meshheading:10321728-Molecular Sequence Data,
pubmed-meshheading:10321728-NF-kappa B,
pubmed-meshheading:10321728-Peptide Synthases,
pubmed-meshheading:10321728-Phosphorylation,
pubmed-meshheading:10321728-Protein Binding,
pubmed-meshheading:10321728-Protein Processing, Post-Translational,
pubmed-meshheading:10321728-SKP Cullin F-Box Protein Ligases,
pubmed-meshheading:10321728-Sequence Homology, Amino Acid,
pubmed-meshheading:10321728-Trans-Activators,
pubmed-meshheading:10321728-Transcriptional Activation,
pubmed-meshheading:10321728-Ubiquitin-Protein Ligases,
pubmed-meshheading:10321728-beta Catenin,
pubmed-meshheading:10321728-beta-Transducin Repeat-Containing Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and beta-catenin.
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pubmed:affiliation |
Derald H Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York, NY 10029-6574, 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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