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

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...

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Veröffentlicht in:	The EMBO journal 2017-08, Vol.36 (15), p.2296-2309
Hauptverfasser:	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:	Artikel
Sprache:	eng
Schlagworte:	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
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