TY - JOUR T1 - Oxidized lipids keep heat shock chaperones busy: new insights on the deficiencies of tumour-associated dendritic cells JF - Journal for ImmunoTherapy of Cancer JO - J Immunother Cancer DO - 10.1186/s40425-018-0373-3 VL - 6 IS - 1 SP - 60 AU - Paula Nunes-Hasler Y1 - 2018/12/01 UR - http://jitc.bmj.com/content/6/1/60.abstract N2 - In a recent publication in Nature Communications the group of Dr. Dmitry Gabrilovich takes us one step closer to understanding why lipid accumulation impairs the function of tumour-associated dendritic cells (DCs). In this study, the authors present two surprising and significant findings. First, they show that in mouse DCs oxidized lipids function as a sink that traps the heat shock chaperone HSP70, a molecular target of emerging anti-cancer strategies. Secondly, they find that HSP70 in turn regulates the trafficking of peptide-loaded major histocompatibility complex class I (pMHC-I) molecules, a complex that triggers the proliferation of cancer-killing T cells. These observations are discussed briefly in the context of lipid droplet function and pMHC-I trafficking in tumour-associated DCs, as well as HSP70’s pleiotropic and incompletely understood roles - and what they mean for future cancer therapy designs.Abbreviations:AQP2Aquaporin-2DCDendritic cellHIVHuman immunodeficiency virusHSP70Heat-shock protein 70 (also called Hspa1a/Hsp72)IL-10Interleukin 10LOX-1Lectin-like oxidized low-density lipoprotein receptor 1MHC-IMajor histocompatibility complex class IOx-trOxidatively truncatedPD-L1Programmed death ligand 1pMHC-IPeptide-loaded major histocompatibility complex class ISNARESoluble N-ethylmaleimide-sensitive factor attachment protein receptorTATTransactivator of transcriptionTLRToll-like receptor ER -