Cargando…

The Role of Protein Tyrosine Phosphatases in Inflammasome Activation

Inflammasomes are multi-protein complexes that mediate the activation and secretion of the inflammatory cytokines IL-1β and IL-18. More than half a decade ago, it has been shown that the inflammasome adaptor molecule, ASC requires tyrosine phosphorylation to allow effective inflammasome assembly and...

Descripción completa

Detalles Bibliográficos
Autores principales: Spalinger, Marianne R., Schwarzfischer, Marlene, Scharl, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7432435/
https://www.ncbi.nlm.nih.gov/pubmed/32751912
http://dx.doi.org/10.3390/ijms21155481
_version_ 1783571797563670528
author Spalinger, Marianne R.
Schwarzfischer, Marlene
Scharl, Michael
author_facet Spalinger, Marianne R.
Schwarzfischer, Marlene
Scharl, Michael
author_sort Spalinger, Marianne R.
collection PubMed
description Inflammasomes are multi-protein complexes that mediate the activation and secretion of the inflammatory cytokines IL-1β and IL-18. More than half a decade ago, it has been shown that the inflammasome adaptor molecule, ASC requires tyrosine phosphorylation to allow effective inflammasome assembly and sustained IL-1β/IL-18 release. This finding provided evidence that the tyrosine phosphorylation status of inflammasome components affects inflammasome assembly and that inflammasomes are subjected to regulation via kinases and phosphatases. In the subsequent years, it was reported that activation of the inflammasome receptor molecule, NLRP3, is modulated via tyrosine phosphorylation as well, and that NLRP3 de-phosphorylation at specific tyrosine residues was required for inflammasome assembly and sustained IL-1β/IL-18 release. These findings demonstrated the importance of tyrosine phosphorylation as a key modulator of inflammasome activity. Following these initial reports, additional work elucidated that the activity of several inflammasome components is dictated via their phosphorylation status. Particularly, the action of specific tyrosine kinases and phosphatases are of critical importance for the regulation of inflammasome assembly and activity. By summarizing the currently available literature on the interaction of tyrosine phosphatases with inflammasome components we here provide an overview how tyrosine phosphatases affect the activation status of inflammasomes.
format Online
Article
Text
id pubmed-7432435
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-74324352020-08-24 The Role of Protein Tyrosine Phosphatases in Inflammasome Activation Spalinger, Marianne R. Schwarzfischer, Marlene Scharl, Michael Int J Mol Sci Review Inflammasomes are multi-protein complexes that mediate the activation and secretion of the inflammatory cytokines IL-1β and IL-18. More than half a decade ago, it has been shown that the inflammasome adaptor molecule, ASC requires tyrosine phosphorylation to allow effective inflammasome assembly and sustained IL-1β/IL-18 release. This finding provided evidence that the tyrosine phosphorylation status of inflammasome components affects inflammasome assembly and that inflammasomes are subjected to regulation via kinases and phosphatases. In the subsequent years, it was reported that activation of the inflammasome receptor molecule, NLRP3, is modulated via tyrosine phosphorylation as well, and that NLRP3 de-phosphorylation at specific tyrosine residues was required for inflammasome assembly and sustained IL-1β/IL-18 release. These findings demonstrated the importance of tyrosine phosphorylation as a key modulator of inflammasome activity. Following these initial reports, additional work elucidated that the activity of several inflammasome components is dictated via their phosphorylation status. Particularly, the action of specific tyrosine kinases and phosphatases are of critical importance for the regulation of inflammasome assembly and activity. By summarizing the currently available literature on the interaction of tyrosine phosphatases with inflammasome components we here provide an overview how tyrosine phosphatases affect the activation status of inflammasomes. MDPI 2020-07-31 /pmc/articles/PMC7432435/ /pubmed/32751912 http://dx.doi.org/10.3390/ijms21155481 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Spalinger, Marianne R.
Schwarzfischer, Marlene
Scharl, Michael
The Role of Protein Tyrosine Phosphatases in Inflammasome Activation
title The Role of Protein Tyrosine Phosphatases in Inflammasome Activation
title_full The Role of Protein Tyrosine Phosphatases in Inflammasome Activation
title_fullStr The Role of Protein Tyrosine Phosphatases in Inflammasome Activation
title_full_unstemmed The Role of Protein Tyrosine Phosphatases in Inflammasome Activation
title_short The Role of Protein Tyrosine Phosphatases in Inflammasome Activation
title_sort role of protein tyrosine phosphatases in inflammasome activation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7432435/
https://www.ncbi.nlm.nih.gov/pubmed/32751912
http://dx.doi.org/10.3390/ijms21155481
work_keys_str_mv AT spalingermarianner theroleofproteintyrosinephosphatasesininflammasomeactivation
AT schwarzfischermarlene theroleofproteintyrosinephosphatasesininflammasomeactivation
AT scharlmichael theroleofproteintyrosinephosphatasesininflammasomeactivation
AT spalingermarianner roleofproteintyrosinephosphatasesininflammasomeactivation
AT schwarzfischermarlene roleofproteintyrosinephosphatasesininflammasomeactivation
AT scharlmichael roleofproteintyrosinephosphatasesininflammasomeactivation