Unconventional post-translational modifications in immunological signaling

Immune system proteins are subject to numerous post-translational modifications. In this Focus Review, Mowen and David describe the key 'non-conventional' modifications such as acetylation and nitrosylation that affect immunologically-relevant proteins. The activity of a cell is governed b...

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Published inNature immunology Vol. 15; no. 6; pp. 512 - 520
Main Authors Mowen, Kerri A, David, Michael
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.06.2014
Nature Publishing Group
Subjects
631/250/516
Acetylation
Acetyltransferases - immunology
Animals
Biomedicine
Cell Differentiation - immunology
Cellular signal transduction
Genetic aspects
Health aspects
Humans
Hydrolases - genetics
Hydrolases - immunology
Immune response
Immune system
Immune System - immunology
Immunology
Infectious Diseases
Methylation
Methyltransferases - immunology
Mice
Phosphorylation
Physiological aspects
Post-translational modification
Protein Processing, Post-Translational - genetics
Protein Processing, Post-Translational - immunology
Protein-Arginine Deiminases
Protein-Arginine N-Methyltransferases - genetics
Protein-Arginine N-Methyltransferases - immunology
Receptor, Interferon alpha-beta - immunology
Residues
review-article
Signal Transduction - immunology
Online AccessGet full text
ISSN1529-2908
1529-2916
1529-2916
DOI10.1038/ni.2873

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Abstract Immune system proteins are subject to numerous post-translational modifications. In this Focus Review, Mowen and David describe the key 'non-conventional' modifications such as acetylation and nitrosylation that affect immunologically-relevant proteins. The activity of a cell is governed by the signals it receives from the extracellular milieu, which are 'translated' into the appropriate biological output, such as activation, survival, proliferation, migration or differentiation. Signaling pathways are responsible for converting environmental cues into discrete intracellular events. The alteration of existing proteins by post-translational modification (PTM) is a key feature of signal-transduction pathways that allows the modulation of protein function. Research into PTMs has long been dominated by the investigation of protein phosphorylation; other PTMs, such as methylation of lysine and arginine residues, acetylation, and nitrosylation of thiol groups and tyrosine residues, have received comparatively little attention. This Review aims to present an overview of these PTMs, with an emphasis on their role in cells of the immune system.
AbstractList The activity of a cell is governed by the signals it receives from the extracellular milieu, which are 'translated' into the appropriate biological output, such as activation, survival, proliferation, migration or differentiation. Signaling pathways are responsible for converting environmental cues into discrete intracellular events. The alteration of existing proteins by post-translational modification (PTM) is a key feature of signal-transduction pathways that allows the modulation of protein function. Research into PTMs has long been dominated by the investigation of protein phosphorylation; other PTMs, such as methylation of lysine and arginine residues, acetylation, and nitrosylation of thiol groups and tyrosine residues, have received comparatively little attention. This Review aims to present an overview of these PTMs, with an emphasis on their role in cells of the immune system.
The activity of a cell is governed by the signals it receives from the extracellular milieu, which are 'translated' into the appropriate biological output, such as activation, survival, proliferation, migration or differentiation. Signaling pathways are responsible for converting environmental cues into discrete intracellular events. The alteration of existing proteins by post-translational modification (PTM) is a key feature of signal-transduction pathways that allows the modulation of protein function. Research into PTMs has long been dominated by the investigation of protein phosphorylation; other PTMs, such as methylation of lysine and arginine residues, acetylation, and nitrosylation of thiol groups and tyrosine residues, have received comparatively little attention. This Review aims to present an overview of these PTMs, with an emphasis on their role in cells of the immune system.The activity of a cell is governed by the signals it receives from the extracellular milieu, which are 'translated' into the appropriate biological output, such as activation, survival, proliferation, migration or differentiation. Signaling pathways are responsible for converting environmental cues into discrete intracellular events. The alteration of existing proteins by post-translational modification (PTM) is a key feature of signal-transduction pathways that allows the modulation of protein function. Research into PTMs has long been dominated by the investigation of protein phosphorylation; other PTMs, such as methylation of lysine and arginine residues, acetylation, and nitrosylation of thiol groups and tyrosine residues, have received comparatively little attention. This Review aims to present an overview of these PTMs, with an emphasis on their role in cells of the immune system.
Immune system proteins are subject to numerous post-translational modifications. In this Focus Review, Mowen and David describe the key 'non-conventional' modifications such as acetylation and nitrosylation that affect immunologically-relevant proteins. The activity of a cell is governed by the signals it receives from the extracellular milieu, which are 'translated' into the appropriate biological output, such as activation, survival, proliferation, migration or differentiation. Signaling pathways are responsible for converting environmental cues into discrete intracellular events. The alteration of existing proteins by post-translational modification (PTM) is a key feature of signal-transduction pathways that allows the modulation of protein function. Research into PTMs has long been dominated by the investigation of protein phosphorylation; other PTMs, such as methylation of lysine and arginine residues, acetylation, and nitrosylation of thiol groups and tyrosine residues, have received comparatively little attention. This Review aims to present an overview of these PTMs, with an emphasis on their role in cells of the immune system.
Audience Academic
Author David, Michael
Mowen, Kerri A
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  email: midavid@ucsd.edu
  organization: Division of Biological Sciences, Section of Molecular Biology, University of California San Diego, La Jolla, CA, USA, Moores Cancer Center, University of California San Diego
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PublicationTitle Nature immunology
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PublicationYear 2014
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Snippet Immune system proteins are subject to numerous post-translational modifications. In this Focus Review, Mowen and David describe the key 'non-conventional'...
The activity of a cell is governed by the signals it receives from the extracellular milieu, which are 'translated' into the appropriate biological output,...
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StartPage 512
SubjectTerms 631/250/516
Acetylation
Acetyltransferases - immunology
Animals
Biomedicine
Cell Differentiation - immunology
Cellular signal transduction
Genetic aspects
Health aspects
Humans
Hydrolases - genetics
Hydrolases - immunology
Immune response
Immune system
Immune System - immunology
Immunology
Infectious Diseases
Methylation
Methyltransferases - immunology
Mice
Phosphorylation
Physiological aspects
Post-translational modification
Protein Processing, Post-Translational - genetics
Protein Processing, Post-Translational - immunology
Protein-Arginine Deiminases
Protein-Arginine N-Methyltransferases - genetics
Protein-Arginine N-Methyltransferases - immunology
Receptor, Interferon alpha-beta - immunology
Residues
review-article
Signal Transduction - immunology
Title Unconventional post-translational modifications in immunological signaling
URI https://link.springer.com/article/10.1038/ni.2873
https://www.ncbi.nlm.nih.gov/pubmed/24840982
https://www.proquest.com/docview/1657330295
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Volume 15
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