Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin

Catherine W. Morgans, Ron R. Kopito

Research output: Contribution to journalArticlepeer-review

45 Scopus citations


The 89 kDa NH2-terminal domain of erythrocyte ankyrin is composed almost entirely of 22 tandem repeats of a 33 amino acid sequence and constitutes the binding site for the cytoplasmic NH2-terminal domain of the erythrocyte anion exchanger, AE1. We have developed an assay to evaluate the in vivo interaction between a fragment of ankyrin corresponding to this domain (ANK90) and two non-erythroid anion exchangers, AE2 and AE3, that share considerable structural homology with AE1. Association was assessed by coimmunoprecipitation of ANK90-anion exchanger complexes from detergent extracts of cells cotransfected with plasmids encoding the ankyrin fragment and the anion exchanger or mutants thereof. ANK90 was coimmunoprecipitated with AE1 but not with an AE1 deletion mutant lacking the cytoplasmic NH2-terminal domain. Using this assay, we show that the brain anion exchanger AE3, but not the closely related homologue, AE2, is capable of binding to ankyrin.

Original languageEnglish (US)
Pages (from-to)1137-1142
Number of pages6
JournalJournal of Cell Science
Issue number4
StatePublished - Aug 1993
Externally publishedYes


  • Anion exchanger
  • Ankyrin
  • Membrane skeleton

ASJC Scopus subject areas

  • Cell Biology


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