ArticleThe Journal of biological chemistry2011
Dual transport properties of anion exchanger 1: the same transmembrane segment is involved in anion exchange and in a cation leak.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Mechanisms of NaFrontiers in physiology · 2022Review
- Membrane Transporters and Channels in Melanoma.Reviews of physiology, biochemistry and pharmacology · 2021Review
- Review
- Does aberrant membrane transport contribute to poor outcome in adult acute myeloid leukemia?Frontiers in pharmacology · 2015Article
- Structure and Function of SLC4 Family [Formula: see text] Transporters.Frontiers in physiology · 2015Article
- Expansion of the APC superfamily of secondary carriers.Proteins · 2014Article
- pH sensing and regulation in cancer.Frontiers in physiology · 2013Review
- Structural model of the anion exchanger 1 (SLC4A1) and identification of transmembrane segments forming the transport site.The Journal of biological chemistry · 2013Article
- Substitution of transmembrane domain Cys residues alters pH(o)-sensitive anion transport by AE2/SLC4A2 anion exchanger.Pflugers Archiv : European journal of physiology · 2013Article
- Band 3 missense mutations and stomatocytosis: insight into the molecular mechanism responsible for monovalent cation leak.International journal of cell biology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous results suggested that specific point mutations in human anion exchanger 1 (AE1) convert the electroneutral anion exchanger into a monovalent cation conductance. In the present study, the transport site for anion exchange and for the cation leak has been studied by cysteine scanning mutagenesis and sulfhydryl reagent chemistry. Moreover, the role of some highly conserved amino acids within members of the SLC4 family to which AE1 belongs has been assessed in AE1 transport properties. The results suggest that the same transport site within the AE1 spanning domain is involved in anion exchange or in cation transport. A functioning mechanism for this transport site is proposed according to transport properties of the different studied point mutations of AE1.
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