The role of s-palmitoylation in neurological diseases: implication for zDHHC family

S-palmitoylation is a reversible posttranslational modification, and the palmitoylation reaction in human-derived cells is mediated by the zDHHC family, which is composed of S-acyltransferase enzymes that possess the DHHC (Asp-His-His-Cys) structural domain. zDHHC proteins form an autoacylation inte...

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Published inFrontiers in pharmacology Vol. 14; p. 1342830
Main Authors Liao, Dan, Huang, Yutao, Liu, Dan, Zhang, Haofuzi, Shi, Xinyu, Li, Xin, Luo, Peng
Format Journal Article
LanguageEnglish
Published Switzerland Frontiers Media S.A 16.01.2024
Subjects
glutamate receptor
neurological diseases
Pharmacology
protein acyltransferase
S-palmitoylation
scaffold protein
zDHHC
S-palmitoylation
scaffold protein
neurological diseases
protein acyltransferase
glutamate receptor
zDHHC
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Summary:S-palmitoylation is a reversible posttranslational modification, and the palmitoylation reaction in human-derived cells is mediated by the zDHHC family, which is composed of S-acyltransferase enzymes that possess the DHHC (Asp-His-His-Cys) structural domain. zDHHC proteins form an autoacylation intermediate, which then attaches the fatty acid to cysteine a residue in the target protein. zDHHC proteins sublocalize in different neuronal structures and exert dif-ferential effects on neurons. In humans, many zDHHC proteins are closely related to human neu-rological disor-ders. This review focuses on a variety of neurological disorders, such as AD (Alz-heimer's disease), HD (Huntington's disease), SCZ (schizophrenia), XLID (X-linked intellectual disability), attention deficit hyperactivity disorder and glioma. In this paper, we will discuss and summarize the research progress regarding the role of zDHHC proteins in these neu-rological disorders.
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Reviewed by: Johannes W. Hell, University of California, Davis, United States
Seyyedmohsen Hosseinibarkooie, University Hospital of Cologne, Germany
Edited by: Liu Qing-Shan, Minzu University of China, China
These authors have contributed equally to this work
ISSN:1663-9812
1663-9812
DOI:10.3389/fphar.2023.1342830