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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2010-8-4
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pubmed:databankReference |
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pubmed:abstractText |
Ubiquitin is a versatile cellular signaling molecule that can form polymers of eight different linkages, and individual linkage types have been associated with distinct cellular functions. Though little is currently known about Lys11-linked ubiquitin chains, recent data indicate that they may be as abundant as Lys48 linkages and may be involved in vital cellular processes. Here we report the generation of Lys11-linked polyubiquitin in vitro, for which the Lys11-specific E2 enzyme UBE2S was fused to a ubiquitin binding domain. Crystallographic and NMR analyses of Lys11-linked diubiquitin reveal that Lys11-linked chains adopt compact conformations in which Ile44 is solvent exposed. Furthermore, we identify the OTU family deubiquitinase Cezanne as the first deubiquitinase with Lys11-linkage preference. Our data highlight the intrinsic specificity of the ubiquitin system that extends to Lys11-linked chains and emphasize that differentially linked polyubiquitin chains must be regarded as independent post-translational modifications.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20622874-10089880,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20622874-9759494
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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 |
Aug
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pubmed:issn |
1545-9985
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
939-47
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pubmed:dateRevised |
2011-7-22
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pubmed:meshHeading |
pubmed-meshheading:20622874-Crystallography, X-Ray,
pubmed-meshheading:20622874-Endopeptidases,
pubmed-meshheading:20622874-Humans,
pubmed-meshheading:20622874-Hydrolysis,
pubmed-meshheading:20622874-Lysine,
pubmed-meshheading:20622874-Magnetic Resonance Spectroscopy,
pubmed-meshheading:20622874-Protein Structure, Quaternary,
pubmed-meshheading:20622874-Protein Structure, Tertiary,
pubmed-meshheading:20622874-Reproducibility of Results,
pubmed-meshheading:20622874-Solutions,
pubmed-meshheading:20622874-Substrate Specificity,
pubmed-meshheading:20622874-Ubiquitin,
pubmed-meshheading:20622874-Ubiquitin-Conjugating Enzymes,
pubmed-meshheading:20622874-Ubiquitination
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pubmed:year |
2010
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pubmed:articleTitle |
Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne.
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pubmed:affiliation |
Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
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pubmed:publicationType |
Journal Article
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