ORIGINAL RESEARCH published: 02 March 2017 doi: 10.3389/fimmu.2017.00222 The Function of FK506-Binding Protein 13 in Protein Quality Control Protects Plasma Cells from Endoplasmic Reticulum Stress- Edited by: Associated Apoptosis Harry W. Schroeder, University of Alabama at Birmingham, 1† 1 1 2 3 USA Mini Jeong , Eunkyeong Jang , Suk San Choi , Changhoon Ji , Kyungho Lee and Jeehee Youn1* Reviewed by: Michael A. Lynes, 1 Laboratory of Autoimmunology, Department of Anatomy and Cell Biology, College of Medicine, Hanyang University, Seoul, University of Connecticut, USA South Korea, 2 Protein Metabolism Medical Research Center, Department of Biomedical Sciences, College of Medicine, Thierry Defrance, Seoul National University, Seoul, South Korea, 3 Department of Biological Sciences, Konkuk University, Seoul, South Korea Institut national de la santé et de la recherche médicale (INSERM), France Plasma cells (PCs) are exposed to intense endoplasmic reticulum (ER) stress imposed *Correspondence: by enormous rates of immunoglobulin (Ig) synthesis and secretion. Therefore, protein Jeehee Youn
[email protected] homeostasis is crucial for the survival of PCs, but its molecular mechanism remains largely unknown. Here, we found marked overexpression of FK506-binding protein 13 †Present address: Mini Jeong, (FKBP13) in long-lived PCs from autoimmune mice and investigated its function using Department of Biochemistry and a plasmacytoma cell line secreting IgA. FKBP13 expression was induced largely in the Molecular Biology, Korean Institute of Molecular Medicine and Nutrition, lumen of ER in response to treatment with an ER stressor tunicamycin or overexpression Korea University College of Medicine, of an adaptive unfolded protein response (UPR) protein X-box binding protein 1 (XBP1).