Title

Histone citrullination by protein arginine deiminase: is arginine methylation a green light or a roadblock

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Publication Date

8-22-2006

Document Type

Article

Subjects

Arginine; Chemistry; Citrulline; *Gene Expression Regulation, Enzymologic; Histones; Hydrolases; Methylation; Models, Chemical; Models, Molecular; Multigene Family; Protein Conformation; Protein Processing, Post-Translational; Proteomics

Disciplines

Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics

Abstract

Protein citrullination, a once-obscure post-translational modification (PTM) of peptidylarginine, has recently become an area of significant interest because of its suspected role in human disease states, including rheumatoid arthritis and multiple sclerosis, and also because of its newfound role in gene regulation. One protein isozyme responsible for this modification, protein arginine deiminase 4 (PAD4), has also been proposed to "reverse" epigenetic histone modifications made by the protein arginine methyltransferases. Here, we review the in vivo and in vitro studies of transcriptional regulation by PAD4, evaluate conflicting evidence for its ability to use methylated peptidylarginine as a substrate, and highlight promising areas of future work. Understanding the interplay of multiple arginine PTMs is an emerging area of importance in health and disease and is a topic best addressed by novel tools in proteomics and chemical biology.

DOI of Published Version

10.1021/cb6002306

Source

ACS Chem Biol. 2006 Aug 22;1(7):433-41. Link to article on publisher's site

Journal/Book/Conference Title

ACS chemical biology

Comments

At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.

Related Resources

Link to Article in PubMed

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