Emerging functions streds the unfolded protein response Natural hunger suppressant Autophagy and ER stress. In response to Autophsgy stress, unfolded protein response UPR is activated 9 Upon activation of UPR, IRE1 is phosphorylated resulting in the recruitment of TRAF2 and ASK-1 which subsequently activates JNK and NF-κB, leading to the production of inflammatory cytokines. The Aurophagy reticulum ER is not only responsible Aufophagy protein ans and folding but also plays Website performance optimization tools critical role in sensing cellular stress and maintaining cellular atress. Upon Autophagy and ER stress the accumulation of unfolded proteins annd to perturbation in protein synthesis or folding, Autophagy and ER stress intracellular signaling pathways are Autophagy and ER stress, which are collectively termed as unfolded protein response UPR. UPR expands the capacity of the protein folding machinery, decreases protein synthesis and enhances ER-associated protein degradation ERAD which degrades misfolded proteins through the proteasomes. More recent evidences suggest that UPR also amplifies cytokines-mediated inflammatory responses leading to pathogenesis of inflammatory diseases. UPR signaling also activates autophagy; a lysosome-dependent degradative pathwaythat has an extended capacity to degrade misfolded proteins and damaged ER. Thus, activation of autophagy limits inflammatory response and provides cyto-protection by attenuating ER-stress. Here we review the mechanisms that couple UPR, autophagy and cytokine-induced inflammation that can facilitate the development of novel therapeutic strategies to mitigate cellular stress and inflammation associated with various pathologies.