» Articles » PMID: 34725336

Interplay Between ADP-ribosyltransferases and Essential Cell Signaling Pathways Controls Cellular Responses

Overview
Journal Cell Discov
Date 2021 Nov 2
PMID 34725336
Citations 14
Authors
Affiliations
Soon will be listed here.
Abstract

Signaling cascades provide integrative and interactive frameworks that allow the cell to respond to signals from its environment and/or from within the cell itself. The dynamic regulation of mammalian cell signaling pathways is often modulated by cascades of protein post-translational modifications (PTMs). ADP-ribosylation is a PTM that is catalyzed by ADP-ribosyltransferases and manifests as mono- (MARylation) or poly- (PARylation) ADP-ribosylation depending on the addition of one or multiple ADP-ribose units to protein substrates. ADP-ribosylation has recently emerged as an important cell regulator that impacts a plethora of cellular processes, including many intracellular signaling events. Here, we provide an overview of the interplay between the intracellular diphtheria toxin-like ADP-ribosyltransferase (ARTD) family members and five selected signaling pathways (including NF-κB, JAK/STAT, Wnt-β-catenin, MAPK, PI3K/AKT), which are frequently described to control or to be controlled by ADP-ribosyltransferases and how these interactions impact the cellular responses.

Citing Articles

Integrative Multi-PTM Proteomics Reveals Dynamic Global, Redox, Phosphorylation, and Acetylation Regulation in Cytokine-Treated Pancreatic Beta Cells.

Gluth A, Li X, Gritsenko M, Gaffrey M, Kim D, Lalli P Mol Cell Proteomics. 2024; 23(12):100881.

PMID: 39550035 PMC: 11700301. DOI: 10.1016/j.mcpro.2024.100881.


Unleashing viral mimicry: A combinatorial strategy to enhance the efficacy of PARP7 inhibitors.

Manetsch P, Hottiger M Bioessays. 2024; 47(2):e2400087.

PMID: 39502005 PMC: 11755700. DOI: 10.1002/bies.202400087.


Identification of porcine PARP11 as a restricted factor for pseudorabies virus.

Qi C, Zhao D, Wang X, Hu L, Wang Y, Wu H Front Cell Infect Microbiol. 2024; 14:1414827.

PMID: 39445214 PMC: 11496260. DOI: 10.3389/fcimb.2024.1414827.


Crosstalk between BER and NHEJ in XRCC4-Deficient Cells Depending on hTERT Overexpression.

Sergeeva S, Loshchenova P, Oshchepkov D, Orishchenko K Int J Mol Sci. 2024; 25(19).

PMID: 39408734 PMC: 11476898. DOI: 10.3390/ijms251910405.


Poly(ADP-Ribose) Polymerase-1 Regulates Pyroptosis Independent Function of NLRP3 Inflammasome in Neutrophil Extracellular Trap Formation.

Delinois L, Sharma A, Ramesh A, Boatright L, Li Q, Xu R Immunohorizons. 2024; 8(8):586-597.

PMID: 39186692 PMC: 11374751. DOI: 10.4049/immunohorizons.2400058.


References
1.
Larsen S, Hendriks I, Lyon D, Jensen L, Nielsen M . Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation. Cell Rep. 2018; 24(9):2493-2505.e4. DOI: 10.1016/j.celrep.2018.07.083. View

2.
Tong L, Denu J . Function and metabolism of sirtuin metabolite O-acetyl-ADP-ribose. Biochim Biophys Acta. 2010; 1804(8):1617-25. PMC: 3310390. DOI: 10.1016/j.bbapap.2010.02.007. View

3.
Pilie P, Gay C, Byers L, OConnor M, Yap T . PARP Inhibitors: Extending Benefit Beyond -Mutant Cancers. Clin Cancer Res. 2019; 25(13):3759-3771. DOI: 10.1158/1078-0432.CCR-18-0968. View

4.
Jordan J, Landau E, Iyengar R . Signaling networks: the origins of cellular multitasking. Cell. 2000; 103(2):193-200. PMC: 3619409. DOI: 10.1016/s0092-8674(00)00112-4. View

5.
Brady P, Goel A, Johnson M . Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity. Microbiol Mol Biol Rev. 2018; 83(1). PMC: 6383445. DOI: 10.1128/MMBR.00038-18. View