Fuller, W. and Gök, C. (2020) Regulation of NCX1 by palmitoylation. Cell Calcium, 86, 102158. (doi: 10.1016/j.ceca.2019.102158) (PMID:31935590)
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Abstract
Palmitoylation (S-acylation) is the reversible conjugation of a fatty acid (usually C16 palmitate) to intracellular cysteine residues of proteins via a thioester linkage. Palmitoylation anchors intracellular regions of proteins to membranes because the palmitoylated cysteine is recruited to the lipid bilayer. NCX1 is palmitoylated at a single cysteine in its large regulatory intracellular loop. The presence of an amphipathic α-helix immediately adjacent to the NCX1 palmitoylation site is required for NCX1 palmitoylation. The NCX1 palmitoylation site is conserved through most metazoan phlya. Although palmitoylation does not regulate the normal forward or reverse ion transport modes of NCX1, NCX1 palmitoylation is required for its inactivation: sodium-dependent inactivation and inactivation by PIP2 depletion are significantly impaired for unpalmitoylatable NCX1. Here we review the role of palmitoylation in regulating NCX1 activity, and highlight future questions that must be addressed to fully understand the importance of this regulatory mechanism for sodium and calcium transport in cardiac muscle.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Fuller, Professor Will and Gok, Dr Caglar |
Authors: | Fuller, W., and Gök, C. |
College/School: | College of Medical Veterinary and Life Sciences > School of Cardiovascular & Metabolic Health |
Journal Name: | Cell Calcium |
Publisher: | Elsevier |
ISSN: | 0143-4160 |
ISSN (Online): | 1532-1991 |
Published Online: | 08 January 2020 |
Copyright Holders: | Copyright © 2019 Elsevier Ltd. |
First Published: | First published in Cell Calcium 86:102158 |
Publisher Policy: | Reproduced in accordance with the publisher copyright policy |
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