Gök, C. and Fuller, W. (2024) Rise of palmitoylation: a new trick to tune NCX1 activity. Biochimica et Biophysica Acta: Molecular Cell Research, 1871(5), 119719. (doi: 10.1016/j.bbamcr.2024.119719) (PMID:38574822)
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Abstract
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.
Item Type: | Articles |
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Additional Information: | We acknowledge financial support from the British Heart Foundation: grant reference SP/16/3/32317 to WF, PG/22/10847 to WF and CG, Centre of Research Excellence award RE/18/634217. |
Keywords: | NCX1 inactivation, palmitoylation, depalmitoylation, Ca2+ handling, cardiac pathologies. |
Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Fuller, Professor Will and Gok, Dr Caglar |
Authors: | Gök, C., and Fuller, W. |
College/School: | College of Medical Veterinary and Life Sciences > School of Cardiovascular & Metabolic Health |
Journal Name: | Biochimica et Biophysica Acta: Molecular Cell Research |
Publisher: | Elsevier |
ISSN: | 0167-4889 |
ISSN (Online): | 1879-2596 |
Published Online: | 03 April 2024 |
Copyright Holders: | Copyright © 2024 The Authors |
First Published: | First published in Biochimica et Biophysica Acta: Molecular Cell Research 1871(5):119719 |
Publisher Policy: | Reproduced under a Creative Commons License |
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