Highlights
- Protein citrullination has emerged as a potential therapeutic target due to its role in many human pathologies.
- The biological roles of protein citrullination are mostly unknown due to the challenges associated with detecting this PTM.
- The authors highlight the latest detection tools in the field of citrullination.
- The authors describe how citrullination impacts protein function.
Citrullination is a post-translational modification of arginine that is catalyzed by the protein arginine deiminases (PADs). Abnormal citrullination is observed in many autoimmune diseases and cancers. Anti-citrullinated protein antibodies (ACPA) are hallmarks of RA and used as diagnostic markers for disease diagnosis. Even though citrullination is associated with many different pathologies, its role remains unclear due to the challenges associated with the detection of citrullinated proteins since the mass change is only 0.984 Da. Moreover, the functional effects of protein citrullination remain mostly unknown. Herein, we discuss a brief overview of PAD structure and function, recent advances in the detection of citrullinated proteins in complex biological systems and the functional consequences of protein citrullination.