Please use this identifier to cite or link to this item: https://doi.org/10.1186/s12867-016-0065-9
Title: A potential role for protein palmitoylation and zDHHC16 in DNA damage response
Authors: Cao, N
Li, J.-K
Rao, Y.-Q
Liu, H
Wu, J
Li, B
Zhao, P
Zeng, L 
Li, J
Keywords: acyltransferase
ATM protein
protein p53
unclassified drug
zinc finger aspartylhistidylhistidylcystein domain 16 protein
Abelson kinase
ATM protein
Atm protein, mouse
carrier protein
protein p53
Zdhhc16 protein, mouse
animal cell
Article
controlled study
DNA damage
DNA damage response
embryo
enzyme activation
enzyme activity
female
G2 phase cell cycle checkpoint
gene expression
mouse
nonhuman
palmitoylation
protein induction
signal transduction
zDHHC16 gene
animal
apoptosis
C57BL mouse
cell culture
cell cycle checkpoint
cytology
DNA damage
DNA repair
fibroblast
gene deletion
gene inactivation
genetics
lipoylation
metabolism
protein protein interaction
Animals
Apoptosis
Ataxia Telangiectasia Mutated Proteins
Carrier Proteins
Cell Cycle Checkpoints
Cells, Cultured
DNA Damage
DNA Repair
Female
Fibroblasts
Gene Deletion
Gene Knockout Techniques
Lipoylation
Mice, Inbred C57BL
Protein Interaction Maps
Proto-Oncogene Proteins c-abl
Tumor Suppressor Protein p53
Issue Date: 2016
Citation: Cao, N, Li, J.-K, Rao, Y.-Q, Liu, H, Wu, J, Li, B, Zhao, P, Zeng, L, Li, J (2016). A potential role for protein palmitoylation and zDHHC16 in DNA damage response. BMC Molecular Biology 17 (1) : 12. ScholarBank@NUS Repository. https://doi.org/10.1186/s12867-016-0065-9
Rights: Attribution 4.0 International
Abstract: Background: Cells respond to DNA damage by activating the phosphatidylinositol-3 kinase-related kinases, p53 and other pathways to promote cell cycle arrest, apoptosis, and/or DNA repair. Here we report that protein palmitoylation, a modification carried out by protein acyltransferases with zinc-finger and Asp-His-His-Cys domains (zDHHC), is required for proper DNA damage responses. Results: Inhibition of protein palmitoylation compromised DNA damage-induced activation of Atm, induction and activation of p53, cell cycle arrest at G2/M phase, and DNA damage foci assembly/disassembly in primary mouse embryonic fibroblasts. Furthermore, knockout of zDHHC16, a palmitoyltransferase gene identified as an interacting protein for c-Abl, a non-receptor tyrosine kinase involved in DNA damage response, reproduced most of the defects in DNA damage responses produced by the inhibition of protein palmitoylation. Conclusions: Our results revealed critical roles for protein palmitoylation and palmitoyltransferase zDHHC16 in early stages of DNA damage responses and in the regulation of Atm activation. © 2016 Cao et al.
Source Title: BMC Molecular Biology
URI: https://scholarbank.nus.edu.sg/handle/10635/181371
ISSN: 14712199
DOI: 10.1186/s12867-016-0065-9
Rights: Attribution 4.0 International
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