University of Massachusetts Medical School Faculty Publications

Title

Chemical biology of protein citrullination by the protein A arginine deiminases

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology; Program in Chemical Biology; Thompson Lab

Publication Date

2021-03-03

Document Type

Article

Disciplines

Amino Acids, Peptides, and Proteins | Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry

Abstract

Citrullination is a post-translational modification (PTM) that converts peptidyl-arginine into peptidyl-citrulline; citrullination is catalyzed by the protein arginine deiminases (PADs). This PTM is associated with several physiological processes, including the epigenetic regulation of gene expression, neutrophil extracellular trap formation, and DNA-damage induced apoptosis. Notably, aberrant protein citrullination is relevant to several autoimmune and neurodegenerative diseases and certain forms of cancer. As such, the PADs are promising therapeutic targets. In this review, we discuss recent advances in the development of PAD inhibitors and activity-based probes, the development and use of citrulline-specific probes in chemoproteomic applications, and methods to site-specifically incorporate citrulline into proteins.

Keywords

Activity-based protein profiling, Autocitrullination, Citrulline incorporation, Inhibitor, Post-translational modifications, Protein arginine deiminase (PAD)

DOI of Published Version

10.1016/j.cbpa.2021.01.010

Source

Mondal S, Thompson PR. Chemical biology of protein citrullination by the protein A arginine deiminases. Curr Opin Chem Biol. 2021 Mar 3;63:19-27. doi: 10.1016/j.cbpa.2021.01.010. Epub ahead of print. PMID: 33676233. Link to article on publisher's site

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

Current opinion in chemical biology

PubMed ID

33676233

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