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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
38
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pubmed:dateCreated |
2001-9-18
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pubmed:abstractText |
The involvement of red blood cell spectrin in the ubiquitination process was studied. Spectrin was found to form two ubiquitin-associated derivatives, a DTT-sensitive ubiquitin adduct and a DTT-insensitive conjugate, characteristic intermediate and final products of the ubiquitination reaction cascade. In addition to spectrin and ubiquitin, ubiquitin-activating enzyme (E1) and ATP were necessary and sufficient to form both the spectrin-ubiquitin adduct and conjugate. No exogenous ubiquitin-conjugating (E2) or ligase (E3) activities were required, suggesting that erythrocyte spectrin is an E2 ubiquitin-conjugating enzyme able to target itself. Both ubiquitin adduct and conjugate were linked to the alpha subunit of spectrin, suggesting that the ubiquitin-conjugating (UBC) domain and its target regions reside on the same subunit.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-2960
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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 |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11630-42
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11560514-Adenosine Triphosphate,
pubmed-meshheading:11560514-Amino Acid Sequence,
pubmed-meshheading:11560514-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11560514-Erythrocyte Membrane,
pubmed-meshheading:11560514-Humans,
pubmed-meshheading:11560514-Ligases,
pubmed-meshheading:11560514-Mass Spectrometry,
pubmed-meshheading:11560514-Molecular Sequence Data,
pubmed-meshheading:11560514-Molecular Weight,
pubmed-meshheading:11560514-Peptide Fragments,
pubmed-meshheading:11560514-Spectrin,
pubmed-meshheading:11560514-Ubiquitin-Conjugating Enzymes,
pubmed-meshheading:11560514-Ubiquitins
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pubmed:year |
2001
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pubmed:articleTitle |
Erythrocyte spectrin is an E2 ubiquitin conjugating enzyme.
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pubmed:affiliation |
Department of Cell Biology and Neuroscience, University of South Alabama College of Medicine, Mobile, Alabama 36688, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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