ArticleThe Biochemical journal2012
Characterization of cytoskeletal protein 4.1R interaction with NHE1 (Na(+)/H(+) exchanger isoform 1).
Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Tubulin-mediated anatomical and functional changes caused by CaJournal of physiology and biochemistry · 2023Article
- The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells.Frontiers in physiology · 2018Review
- The human Kell blood group binds the erythroid 4.1R protein: new insights into the 4.1R-dependent red cell membrane complex.British journal of haematology · 2015Article
- Na+-H+ exchanger-1 (NHE1) regulation in kidney proximal tubule.Cellular and molecular life sciences : CMLS · 2015Review
- DAL-1 attenuates epithelial-to mesenchymal transition in lung cancer.Journal of experimental & clinical cancer research : CR · 2015Article
- A 130-kDa protein 4.1B regulates cell adhesion, spreading, and migration of mouse embryo fibroblasts by influencing actin cytoskeleton organization.The Journal of biological chemistry · 2014Article
- Article
- Calcium in red blood cells-a perilous balance.International journal of molecular sciences · 2013Review
- Strain-specific variations in cation content and transport in mouse erythrocytes.Physiological genomics · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
NHE1 (Na(+)/H(+) exchanger isoform 1) has been reported to be hyperactive in 4.1R-null erythrocytes [Rivera, De Franceschi, Peters, Gascard, Mohandas and Brugnara (2006) Am. J. Physiol. Cell Physiol. 291, C880-C886], supporting a functional interaction between NHE1 and 4.1R. In the present paper we demonstrate that 4.1R binds directly to the NHE1cd (cytoplasmic domain of NHE1) through the interaction of an EED motif in the 4.1R FERM (4.1/ezrin/radixin/moesin) domain with two clusters of basic amino acids in the NHE1cd, K(519)R and R(556)FNKKYVKK, previously shown to mediate PIP(2) (phosphatidylinositol 4,5-bisphosphate) binding [Aharonovitz, Zaun, Balla, York, Orlowski and Grinstein (2000) J. Cell. Biol. 150, 213-224]. The affinity of this interaction (K(d) = 100-200 nM) is reduced in hypertonic and acidic conditions, demonstrating that this interaction is of an electrostatic nature. The binding affinity is also reduced upon binding of Ca(2+)/CaM (Ca(2+)-saturated calmodulin) to the 4.1R FERM domain. We propose that 4.1R regulates NHE1 activity through a direct protein-protein interaction that can be modulated by intracellular pH and Na(+) and Ca(2+) concentrations.
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