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  • Title: Erythrocyte spectrin is an E2 ubiquitin conjugating enzyme.
    Author: Kakhniashvili DG, Chaudhary T, Zimmer WE, Bencsath FA, Jardine I, Goodman SR.
    Journal: Biochemistry; 2001 Sep 25; 40(38):11630-42. PubMed ID: 11560514.
    Abstract:
    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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