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. 2020 Nov:91:102254.
doi: 10.1016/j.ceca.2020.102254. Epub 2020 Jul 17.

Palmitoylation: A new mechanism for control of NCX1 function

Elton Veseli  1 , Jonathan Soboloff  2
Affiliations

Palmitoylation: A new mechanism for control of NCX1 function

Elton Veseli et al. Cell Calcium. 2020 Nov.

Abstract

A paper by Gök et al., identified Zinc Finger DHHC-Type Palmitoyltransferase 5 (zDHHC5) and Acyl-Protein Transferase 1 (APT1) as the enzymes responsible for the dynamic palmitoylation of NCX1. Palmitoylation occurs at the cell surface and increases the affinity of NCX1 for lipid rafts. Additionally, they discovered that palmitoylation controls the affinity of NCX1 for exchange inhibitory protein (XIP) and regulates intracellular calcium concentration. These findings provide new insights into endogenous control of NCX1 function and will drive future investigations directed at understanding its full potential.

Keywords: APT1; NCX1; Palmitoylation; zDHHC5.

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Figures

Figure 1:
Figure 1:. The effect of palmitoylation and depalmitoylation of NCX1 on calcium efflux.
Palmitoylation of NCX1 by zDHHC5 at the cell surface alters the structure of and inactivates NCX1 to prevent calcium efflux. APT1 depalmitoylates NCX1 and allows calcium to flow out of the cell.
See this image and copyright information in PMC

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