|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
1994-10-19
|
|
pubmed:abstractText |
We demonstrate an essential role for the proteasome complex in two proteolytic processes required for activation of the transcription factor NF-kappa B. The p105 precursor of the p50 subunit of NF-kappa B is processed in vitro by an ATP-dependent process that requires proteasomes and ubiquitin conjugation. The C-terminal region of p105 is rapidly degraded, leaving the N-terminal p50 domain. p105 processing can be blocked in intact cells with inhibitors of the proteasome or in yeast with proteasome mutants. These inhibitors also block the activation of NF-kappa B and the rapid degradation of I kappa B alpha induced by tumor necrosis factor alpha. Thus, the ubiquitin-proteasome pathway functions not only in the complete degradation of polypeptides, but also in the regulated processing of precursors into active proteins.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Leupeptins,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B p50 Subunit,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappaB inhibitor alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/acetylleucyl-leucyl-norleucinal,
http://linkedlifedata.com/resource/pubmed/chemical/benzyloxycarbonylleucyl-leucyl-leuci...,
http://linkedlifedata.com/resource/pubmed/chemical/carbobenzoxy-leucyl-leucyl-norvalina...
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
0092-8674
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
9
|
|
pubmed:volume |
78
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
773-85
|
|
pubmed:dateRevised |
2007-11-14
|
|
pubmed:meshHeading |
pubmed-meshheading:8087845-Adenosine Triphosphate,
pubmed-meshheading:8087845-Amino Acid Sequence,
pubmed-meshheading:8087845-Animals,
pubmed-meshheading:8087845-Cells, Cultured,
pubmed-meshheading:8087845-Cysteine Endopeptidases,
pubmed-meshheading:8087845-DNA-Binding Proteins,
pubmed-meshheading:8087845-Humans,
pubmed-meshheading:8087845-I-kappa B Proteins,
pubmed-meshheading:8087845-Leupeptins,
pubmed-meshheading:8087845-Models, Biological,
pubmed-meshheading:8087845-Molecular Sequence Data,
pubmed-meshheading:8087845-Multienzyme Complexes,
pubmed-meshheading:8087845-NF-kappa B,
pubmed-meshheading:8087845-NF-kappa B p50 Subunit,
pubmed-meshheading:8087845-Protease Inhibitors,
pubmed-meshheading:8087845-Proteasome Endopeptidase Complex,
pubmed-meshheading:8087845-Protein Precursors,
pubmed-meshheading:8087845-Protein Processing, Post-Translational,
pubmed-meshheading:8087845-Ubiquitins
|
|
pubmed:year |
1994
|
|
pubmed:articleTitle |
The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B.
|
|
pubmed:affiliation |
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|
