PAD2-Mediated Citrullination Contributes to Efficient Oligodendrocyte Differentiation and Myelination

• Published in: Cell reports (Cambridge) Vol. 27; no. 4; pp. 1090 - 1102.e10
• Main Authors: Falcão, Ana Mendanha, Meijer, Mandy, Scaglione, Antonella, Rinwa, Puneet, Agirre, Eneritz, Liang, Jialiang, Larsen, Sara C., Heskol, Abeer, Frawley, Rebecca, Klingener, Michael, Varas-Godoy, Manuel, Raposo, Alexandre A.S.F., Ernfors, Patrik, Castro, Diogo S., Nielsen, Michael L., Casaccia, Patrizia, Castelo-Branco, Gonçalo
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 23.04.2019; Cell Press
• Subjects: Animals; Cell Differentiation - genetics; Cell Lineage; Cell Nucleus - metabolism; chromatin accessibility; Citrullination; Cytoplasm - metabolism; deamination; Gene Expression Profiling; Mice; multiple sclerosis; myelin; Myelin Sheath - metabolism; oligodendrocytes; Oligodendroglia - cytology; Oligodendroglia - metabolism; PAD2; Padi2; Protein Interaction Maps; Protein-Arginine Deiminase Type 2 - analysis; Protein-Arginine Deiminase Type 2 - metabolism; Protein-Arginine Deiminase Type 2 - physiology; proteomics; SILAC; myelin; proteomics; multiple sclerosis; citrullination; chromatin accessibility; Padi2; oligodendrocytes; PAD2; SILAC; deamination

Citrullination, the deimination of peptidylarginine residues into peptidylcitrulline, has been implicated in the etiology of several diseases. In multiple sclerosis, citrullination is thought to be a major driver of pathology through hypercitrullination and destabilization of myelin. As such, inhibi...