Erythrocyte Spectrin Is an E2 Ubiquitin Conjugating Enzyme

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 casca...

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Bibliographic Details
Published in:Biochemistry (Easton) 2001-09, Vol.40 (38), p.11630-11642
Main Authors: Kakhniashvili, David G, Chaudhary, Tanuja, Zimmer, Warren E, Bencsath, F. Aladar, Jardine, Ian, Goodman, Steven R
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Amino Acid Sequence
Electrophoresis, Polyacrylamide Gel
Erythrocyte Membrane - metabolism
Humans
Ligases - blood
Ligases - chemistry
Ligases - isolation & purification
Mass Spectrometry
Molecular Sequence Data
Molecular Weight
Peptide Fragments - chemistry
Spectrin - chemistry
Spectrin - isolation & purification
Spectrin - metabolism
Ubiquitin-Conjugating Enzymes
Ubiquitins - metabolism
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Summary: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 α subunit of spectrin, suggesting that the ubiquitin-conjugating (UBC) domain and its target regions reside on the same subunit.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi010176t