Erythrocyte Spectrin Is an E2 Ubiquitin Conjugating Enzyme

Citations Over Time

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.

Related Papers

• → Tools to investigate the ubiquitin proteasome system(2017)84 cited
• → Deubiquitinating Enzymes: A New Class of Biological Regulators(1998)266 cited
• → E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer(2005)156 cited
• → Dimeric Ube2g2 simultaneously engages donor and acceptor ubiquitins to form Lys48-linked ubiquitin chains(2014)42 cited
• → Ubiquitin binding proteins protect ubiquitin conjugates from disassembly(2002)56 cited