Source:http://linkedlifedata.com/resource/pubmed/id/18187417
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2008-3-17
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pubmed:abstractText |
The Elongin BC-box protein family includes the von Hippel-Lindau tumor suppressor and suppressor of cytokine signaling proteins, which are substrate recognition subunits of structurally related classes of E3 ubiquitin ligases composed of Elongin C-Elongin B-Cullin 2-Rbx1 (Cul2 ubiquitin ligases) or of Elongin C-Elongin B-Cullin 5-Rbx2 (Cul5 ubiquitin ligases). The Elongin BC complex acts as an adaptor that links a substrate recognition subunit to heterodimers of either Cullin 2 (Cul2) and RING finger protein Rbx1 or Cullin 5 (Cul5) and Rbx2. It has been shown ( Kamura, T., Maenaka, K., Kotoshiba, S., Matsumoto, M., Kohda, D., Conaway, R. C., Conaway, J. W., and Nakayama, K. I. (2004) Genes Dev. 18, 3055-3065 ) that interaction of BC-box proteins with their cognate Cul-Rbx module is determined by specific regions, called Cul2- or Cul5-boxes, located immediately downstream of their BC-boxes. Here, we investigate further the mechanisms governing assembly of BC-box proteins with their specific Cul-Rbx modules. Through purification and characterization of a larger collection of BC-box proteins that serve as substrate recognition subunits of Cul2 and Cul5 ubiquitin ligases and through structure-function studies, we define Cul2- and Cul5-boxes in greater detail. Although it previously appeared that there was little sequence similarity between Cul5- and Cul2-box motifs, analyses of newly identified BC-box proteins reveal that residues conserved in the Cul2-box represent a subset of those conserved in the Cul5-box. The sequence motif LPPhiP, which is conserved in most Cul5-boxes and has been suggested to specify assembly of Cul5 ligases, is compatible with Cul2 interaction. Finally, the spacing between BC- and Cullin-boxes is much more flexible than has been appreciated and can vary from as few as 3 and as many as approximately 80 amino acids. Taken together, our findings shed new light on the mechanisms by which BC-box proteins direct recruitment of Cullin-Rbx modules during reconstitution of ubiquitin ligases.
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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/CUL2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CUL5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cullin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA synthesome,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/RBX1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RNF7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/VHL protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Von Hippel-Lindau Tumor Suppressor...,
http://linkedlifedata.com/resource/pubmed/chemical/elongin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:BradfordWilliam DWD,
pubmed-author:ConawayJoan WJW,
pubmed-author:ConawayRonald CRC,
pubmed-author:FlorensLaurenceL,
pubmed-author:MahrourNawelN,
pubmed-author:Martin-BrownSkylarS,
pubmed-author:RedwineWilliam BWB,
pubmed-author:Staehling-HamptonKarenK,
pubmed-author:SwansonSelene KSK,
pubmed-author:WashburnMichael PMP
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8005-13
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pubmed:meshHeading |
pubmed-meshheading:18187417-Amino Acid Motifs,
pubmed-meshheading:18187417-Carrier Proteins,
pubmed-meshheading:18187417-Cell Line,
pubmed-meshheading:18187417-Cullin Proteins,
pubmed-meshheading:18187417-DNA-Directed DNA Polymerase,
pubmed-meshheading:18187417-Humans,
pubmed-meshheading:18187417-Multienzyme Complexes,
pubmed-meshheading:18187417-Protein Structure, Tertiary,
pubmed-meshheading:18187417-Transcription Factors,
pubmed-meshheading:18187417-Ubiquitin-Protein Ligases,
pubmed-meshheading:18187417-Von Hippel-Lindau Tumor Suppressor Protein
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pubmed:year |
2008
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pubmed:articleTitle |
Characterization of Cullin-box sequences that direct recruitment of Cul2-Rbx1 and Cul5-Rbx2 modules to Elongin BC-based ubiquitin ligases.
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pubmed:affiliation |
Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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