Erythrocyte spectrin is an E2 ubiquitin conjugating enzyme. Academic Article

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.

authors

• Zimmer, Warren

published proceedings

• Biochemistry

author list (cited authors)

• Kakhniashvili, D. G., Chaudhary, T., Zimmer, W. E., Bencsath, F. A., Jardine, I., & Goodman, S. R.

citation count

• 17

complete list of authors

• Kakhniashvili, DG||Chaudhary, T||Zimmer, WE||Bencsath, FA||Jardine, I||Goodman, SR

publication date

• September 2001

publisher

• American Chemical Society (ACS)  Publisher

published in

• Biochemistry  Journal

keywords

• Adenosine Triphosphate
• Amino Acid Sequence
• Electrophoresis, Polyacrylamide Gel
• Erythrocyte Membrane
• Humans
• Ligases
• Mass Spectrometry
• Molecular Sequence Data
• Molecular Weight
• Peptide Fragments
• Spectrin
• Ubiquitin-Conjugating Enzymes
• Ubiquitins

PubMed Central ID

• 11560514

Digital Object Identifier (DOI)

• 10.1021/bi010176t

start page

• 11630

end page

• 11642

volume

• 40

issue

• 38

URL

• http://dx.doi.org/10.1021/bi010176t