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MDPI, International Journal of Molecular Sciences, 22(21), p. 8746, 2020

DOI: 10.3390/ijms21228746

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Deimination, Intermediate Filaments and Associated Proteins

Journal article published in 2020 by Julie Briot, Michel Simon ORCID, Marie-Claire Méchin ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.