Palmitoylation: A new mechanism for control of NCX1 function

Elton Veseli; Jonathan Soboloff

doi:10.1016/j.ceca.2020.102254

Palmitoylation: A new mechanism for control of NCX1 function

Elton Veseli, Jonathan Soboloff

Temple University

Research output: Contribution to journal › Comment/debate

2 Scopus citations

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.

Original language	English
Article number	102254
Pages (from-to)	102254
Journal	Cell Calcium
Volume	91
DOIs	https://doi.org/10.1016/j.ceca.2020.102254
State	Published - Nov 2020

Keywords

APT1
NCX1
Palmitoylation
zDHHC5

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10.1016/j.ceca.2020.102254

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@article{4731d0c3cf8f4dcead48d78f978950ac,

title = "Palmitoylation: A new mechanism for control of NCX1 function",

abstract = "A paper by G{\"o}k 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",

author = "Elton Veseli and Jonathan Soboloff",

note = "Publisher Copyright: {\textcopyright} 2020 Elsevier Ltd",

year = "2020",

month = nov,

doi = "10.1016/j.ceca.2020.102254",

language = "English",

volume = "91",

pages = "102254",

journal = "Cell Calcium",

issn = "0143-4160",

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TY - JOUR

T1 - Palmitoylation

T2 - A new mechanism for control of NCX1 function

AU - Veseli, Elton

AU - Soboloff, Jonathan

PY - 2020/11

Y1 - 2020/11

N2 - 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.

AB - 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.

KW - APT1

KW - NCX1

KW - Palmitoylation

KW - zDHHC5

UR - http://www.scopus.com/inward/record.url?scp=85088389048&partnerID=8YFLogxK

U2 - 10.1016/j.ceca.2020.102254

DO - 10.1016/j.ceca.2020.102254

M3 - Comment/debate

C2 - 32721571

SN - 0143-4160

VL - 91

SP - 102254

JO - Cell Calcium

JF - Cell Calcium

M1 - 102254

ER -

Palmitoylation: A new mechanism for control of NCX1 function

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Keywords

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