The endoplasmic reticulum HSP40 co‐chaperone ERdj3/DNAJB11 assembles and functions as a tetramer

• Published in: The EMBO journal Vol. 36; no. 15; pp. 2296 - 2309
• Main Authors: Chen, Kai‐Chun, Qu, Song, Chowdhury, Saikat, Noxon, Isabelle C, Schonhoft, Joseph D, Plate, Lars, Powers, Evan T, Kelly, Jeffery W, Lander, Gabriel C, Wiseman, R Luke
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.08.2017; Springer Nature B.V; John Wiley and Sons Inc
• Subjects: Agglomeration; Binding; Cell Line; Chaperones; Clonal deletion; Dimers; Electron microscopy; EMBO20; EMBO32; EMBO40; Endoplasmic reticulum; Endoplasmic Reticulum - metabolism; Epithelial Cells - physiology; ERdj3/DNAJB11; extracellular chaperone; Gene deletion; HSP40; HSP40 Heat-Shock Proteins - metabolism; HSP40 Heat-Shock Proteins - ultrastructure; Hsp40 protein; Hsp70 protein; Humans; J‐protein co‐chaperone; Mammalian cells; Microscopy, Electron; Oligomers; Protein Interaction Mapping; Protein Multimerization; Secretion; secretory proteostasis; Stresses; Transmission electron microscopy; ERdj3/DNAJB11; extracellular chaperone; J‐protein co‐chaperone; HSP40; secretory proteostasis

ERdj3/DNAJB11 is an endoplasmic reticulum (ER)‐targeted HSP40 co‐chaperone that performs multifaceted functions involved in coordinating ER and extracellular proteostasis. Here, we show that ERdj3 assembles into a native tetramer that is distinct from the dimeric structure observed for other HSP40 c...