Deimination, Intermediate Filaments and Associated Proteins

Deimination (or citrullination) is a post-translational modification catalyzed by a calcium-dependent enzyme family of five peptidylarginine deiminases (PADs). Deimination is involved in physiological processes (cell differentiation, embryogenesis, innate and adaptive immunity, etc.) and in autoimmu...

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Main Authors: Julie Briot, Michel Simon, Marie-Claire Méchin
Format: Article
Language:English
Published: MDPI AG 2020-11-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:https://www.mdpi.com/1422-0067/21/22/8746
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spelling doaj-afa4f199a4b447b088c33ba05ade41012020-11-25T04:06:19ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-11-01218746874610.3390/ijms21228746Deimination, Intermediate Filaments and Associated ProteinsJulie Briot0Michel Simon1Marie-Claire Méchin2UDEAR, Institut National de la Santé Et de la Recherche Médicale, Université Toulouse III Paul Sabatier, Université Fédérale de Toulouse Midi-Pyrénées, U1056, 31059 Toulouse, FranceUDEAR, Institut National de la Santé Et de la Recherche Médicale, Université Toulouse III Paul Sabatier, Université Fédérale de Toulouse Midi-Pyrénées, U1056, 31059 Toulouse, FranceUDEAR, Institut National de la Santé Et de la Recherche Médicale, Université Toulouse III Paul Sabatier, Université Fédérale de Toulouse Midi-Pyrénées, U1056, 31059 Toulouse, FranceDeimination (or citrullination) is a post-translational modification catalyzed by a calcium-dependent enzyme family of five peptidylarginine deiminases (PADs). Deimination is involved in physiological processes (cell differentiation, embryogenesis, innate and adaptive immunity, etc.) and in autoimmune diseases (rheumatoid arthritis, multiple sclerosis and lupus), cancers and neurodegenerative diseases. Intermediate filaments (IF) and associated proteins (IFAP) are major substrates of PADs. Here, we focus on the effects of deimination on the polymerization and solubility properties of IF proteins and on the proteolysis and cross-linking of IFAP, to finally expose some features of interest and some limitations of citrullinomes.https://www.mdpi.com/1422-0067/21/22/8746citrullinationpost-translational modificationcytoskeletonkeratinfilaggrinpeptidylarginine deiminase
collection DOAJ
language English
format Article
sources DOAJ
author Julie Briot
Michel Simon
Marie-Claire Méchin
spellingShingle Julie Briot
Michel Simon
Marie-Claire Méchin
Deimination, Intermediate Filaments and Associated Proteins
International Journal of Molecular Sciences
citrullination
post-translational modification
cytoskeleton
keratin
filaggrin
peptidylarginine deiminase
author_facet Julie Briot
Michel Simon
Marie-Claire Méchin
author_sort Julie Briot
title Deimination, Intermediate Filaments and Associated Proteins
title_short Deimination, Intermediate Filaments and Associated Proteins
title_full Deimination, Intermediate Filaments and Associated Proteins
title_fullStr Deimination, Intermediate Filaments and Associated Proteins
title_full_unstemmed Deimination, Intermediate Filaments and Associated Proteins
title_sort deimination, intermediate filaments and associated proteins
publisher MDPI AG
series International Journal of Molecular Sciences
issn 1661-6596
1422-0067
publishDate 2020-11-01
description Deimination (or citrullination) is a post-translational modification catalyzed by a calcium-dependent enzyme family of five peptidylarginine deiminases (PADs). Deimination is involved in physiological processes (cell differentiation, embryogenesis, innate and adaptive immunity, etc.) and in autoimmune diseases (rheumatoid arthritis, multiple sclerosis and lupus), cancers and neurodegenerative diseases. Intermediate filaments (IF) and associated proteins (IFAP) are major substrates of PADs. Here, we focus on the effects of deimination on the polymerization and solubility properties of IF proteins and on the proteolysis and cross-linking of IFAP, to finally expose some features of interest and some limitations of citrullinomes.
topic citrullination
post-translational modification
cytoskeleton
keratin
filaggrin
peptidylarginine deiminase
url https://www.mdpi.com/1422-0067/21/22/8746
work_keys_str_mv AT juliebriot deiminationintermediatefilamentsandassociatedproteins
AT michelsimon deiminationintermediatefilamentsandassociatedproteins
AT marieclairemechin deiminationintermediatefilamentsandassociatedproteins
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