DNAJB14 is an endoplasmic reticulum (ER)-localized transmembrane J-protein that serves as a co-chaperone for Hsc70/Hsp70 heat shock proteins 1. The protein spans the ER membrane with its J-domain facing the cytosol, where it specifically binds and recruits Hsc70 chaperones to facilitate protein quality control 2. DNAJB14 plays a crucial role in ER-associated degradation (ERAD) by accelerating the degradation of misfolded membrane proteins, including the cystic fibrosis transmembrane conductance regulator mutant CFTRΔF508, through the ubiquitin-proteasome system 2. Beyond protein degradation, DNAJB14 is essential for tetrameric assembly of K+ channels, including ERG and Kv4.2 channels, through an Hsp70-independent mechanism, and can rescue defective hERG channels associated with long QT syndrome 3. Recent studies reveal additional functions in cellular stress responses, including regulation of mitochondrial proteins like PINK1 under CCCP-mediated stress and involvement in a novel ER-to-cytosol protein reflux mechanism (ERCYS) that promotes cancer cell survival 45. DNAJB14 shows tissue-specific expression, being most abundant in testis, and has been implicated in various disease contexts including ankylosing spondylitis and Alzheimer's disease 267.