Key result
Palmitoylation of the cardiac Na+/Ca2+ Exchanger (NCX1) creates a binding site for the endogenous XIP domain, sensitizing the transporter to inactivation and associating with cardiac pathologies.
This review highlights the role of palmitoylation in regulating the cardiac Na+/Ca2+ Exchanger (NCX1) and its potential implications in cardiac pathologies.
May inform NCX1-targeted therapies in calcium dysregulation; leaves open clinical translation and therapeutic modulation.
The cardiac Na+/Ca2+ Exchanger (NCX1) controls transmembrane calcium flux in numerous tissues. The only reversible post-translational modification established to regulate NCX1 is palmitoylation, which alters the ability of the exchanger to inactivate. Palmitoylation creates a binding site for the endogenous XIP domain, a region of the NCX1 intracellular loop established to inactivate NCX1. The binding site created by NCX1 palmitoylation sensitizes the transporter to XIP. Herein we summarize our recent knowledge on NCX1 palmitoylation and its association with cardiac pathologies, and discuss these findings in the light of the recent cryo-EM structures of human NCX1.
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Gök et al. (2024) conducted a review in Cardiac pathologies. NCX1 palmitoylation was evaluated. Palmitoylation of the cardiac Na+/Ca2+ Exchanger (NCX1) creates a binding site for the endogenous XIP domain, sensitizing the transporter to inactivation and associating with cardiac pathologies.
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