Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin.
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 co-immunoprecipitation 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 co-immunoprecipitated 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.
Mesh Terms:
Anion Transport Proteins, Ankyrins, Antiporters, Base Sequence, Binding Sites, Brain, Cell Line, DNA, Complementary, Humans, Membrane Proteins, Molecular Sequence Data, Repetitive Sequences, Nucleic Acid, Transfection
Anion Transport Proteins, Ankyrins, Antiporters, Base Sequence, Binding Sites, Brain, Cell Line, DNA, Complementary, Humans, Membrane Proteins, Molecular Sequence Data, Repetitive Sequences, Nucleic Acid, Transfection
J. Cell. Sci.
Date: Aug. 01, 1993
PubMed ID: 8227202
View in: Pubmed Google Scholar
Download Curated Data For This Publication
536
Switch View:
- Interactions 2