Spectrin’s chimeric E2/E3 enzymatic activity

Steven Goodman, Rachel Petrofes Chapa, Warren E. Zimmer

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

In this minireview, we cover the discovery of the human erythrocyte α spectrin E2/E3 ubiquitin conjugating/ligating enzymatic activity and the specific cysteines involved. We then discuss the consequences when this activity is partially inhibited in sickle cell disease and the possibility that the same attenuation is occurring in multiple organ dysfunction syndrome. We finish by discussing the reasons for believing that nonerythroid α spectrin isoforms (I and II) also have this activity and the importance of testing this hypothesis. If correct, this would suggest that the nonerythroid spectrin isoforms play a major role in protein ubiquitination in all cell types. This would open new fields in experimental biology focused on uncovering the impact that this enzymatic activity has upon protein–protein interactions, protein turnover, cellular signaling, and many other functions impacted by spectrin, including DNA repair.

Original languageEnglish (US)
Pages (from-to)1039-1049
Number of pages11
JournalExperimental Biology and Medicine
Volume240
Issue number8
DOIs
StatePublished - Aug 19 2015

Fingerprint

Spectrin
Protein Isoforms
Cell signaling
Multiple Organ Failure
Ubiquitination
Sickle Cell Anemia
Ubiquitin
DNA Repair
Cysteine
Proteins
Repair
Erythrocytes
DNA
Testing

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Spectrin’s chimeric E2/E3 enzymatic activity. / Goodman, Steven; Petrofes Chapa, Rachel; Zimmer, Warren E.

In: Experimental Biology and Medicine, Vol. 240, No. 8, 19.08.2015, p. 1039-1049.

Research output: Contribution to journalArticle

Goodman, Steven ; Petrofes Chapa, Rachel ; Zimmer, Warren E. / Spectrin’s chimeric E2/E3 enzymatic activity. In: Experimental Biology and Medicine. 2015 ; Vol. 240, No. 8. pp. 1039-1049.
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