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• W2999203462 abstract "Calcineurin B homologous proteins (CHPs) belong to the EF-hand Ca2+-binding protein (EFCaBP) family. They have multiple important functions including the regulation of the Na+/H+ exchanger 1 (NHE1). The human isoforms CHP1 and CHP2 share high sequence similarity, but have distinct expression profiles with CHP2 levels for instance increased in malignant cells. These CHPs bind Ca2+ with high affinity. Biochemical data indicated that Ca2+ can regulate their functions. Experimental evidence for Ca2+-modulated structural changes was lacking. With a newly established fluorescent probe hydrophobicity (FPH) assay, we detected Ca2+-induced conformational changes in both CHPs. These changes are in line with an opening of their hydrophobic pocket that binds the CHP-binding region (CBD) of NHE1. Whereas the pocket is closed in the absence of Ca2+ in CHP2, it is still accessible for the dye in CHP1. Both CHPs interacted with CBD in the presence and absence of Ca2+. Isothermal titration calorimetry (ITC) analysis revealed high binding affinity for both CHPs to CBD with equilibrium dissociation constants (KDs) in the nanomolar range. The KD for CHP1:CBD was not affected by Ca2+, whereas Ca2+-depletion increased the KD 7-fold for CHP2:CBD showing a decreased affinity. The data indicate an isoform specific regulatory interaction of CHP1 and CHP2 with NHE1." @default.
• W2999203462 created "2020-01-23" @default.
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• W2999203462 date "2020-01-07" @default.
• W2999203462 modified "2023-10-17" @default.
• W2999203462 title "Calcium affects CHP1 and CHP2 conformation and their interaction with sodium/proton exchanger 1" @default.
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• W2999203462 doi "https://doi.org/10.1096/fj.201902093r" @default.
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