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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2006-7-3
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pubmed:abstractText |
F-Box proteins (FBPs) are variable adaptor proteins that earmark protein substrates for ubiquination and destruction by the proteasome. Through their N-terminal F-box motif, they couple specific protein substrates to a catalytic machinery known as SCF (Skp-1/Cul1/F-Box) E3-ubiquitin ligase. Typical FBPs bind the specific substrates in a phosphorylation dependent manner via their C-termini using either leucine rich repeats (LRR) or tryptophan-aspartic acid (WD40) domains for substrate recognition. By using a gene trap strategy that selects for genes induced during programmed cell death, we have isolated the mouse homolog of the hypothetical human F-Box protein 33 (FBX33). Here we identify FBX33 as a component of an SCF E3-ubiquitin ligase that targets the multifunctional regulator Y-box binding protein 1 (YB-1)/dbpB/p50 for polyubiquitination and destruction by the proteasome. By targeting YB-1 for proteasomal degradation, FBX33 negatively interferes with YB-1 mediated functions. In contrast to typical FBPs, FBX33 has no C-terminal LRR or WD40 domains and associates with YB-1 via its N-terminus. The present study confirms the existence of a formerly hypothetical F-Box protein in living cells and describes one of its substrates.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
580
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3921-30
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:16797541-Amino Acid Sequence,
pubmed-meshheading:16797541-Animals,
pubmed-meshheading:16797541-Apoptosis,
pubmed-meshheading:16797541-COS Cells,
pubmed-meshheading:16797541-Cells, Cultured,
pubmed-meshheading:16797541-Cercopithecus aethiops,
pubmed-meshheading:16797541-Humans,
pubmed-meshheading:16797541-Mice,
pubmed-meshheading:16797541-Molecular Sequence Data,
pubmed-meshheading:16797541-Nerve Tissue Proteins,
pubmed-meshheading:16797541-Polyubiquitin,
pubmed-meshheading:16797541-Proteasome Endopeptidase Complex,
pubmed-meshheading:16797541-Protein Binding,
pubmed-meshheading:16797541-Protein Processing, Post-Translational,
pubmed-meshheading:16797541-Protein Structure, Tertiary,
pubmed-meshheading:16797541-RNA, Messenger,
pubmed-meshheading:16797541-SKP Cullin F-Box Protein Ligases,
pubmed-meshheading:16797541-Transcription Factors,
pubmed-meshheading:16797541-Transcriptional Activation,
pubmed-meshheading:16797541-Y-Box-Binding Protein 1
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pubmed:year |
2006
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pubmed:articleTitle |
Proteasomal degradation of the multifunctional regulator YB-1 is mediated by an F-Box protein induced during programmed cell death.
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pubmed:affiliation |
Department for Molecular Hematology, University of Frankfurt Medical School, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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