Newly synthesised secretory and transmembrane proteins are processed by the endoplasmic reticulum (ER). A disruption in this functionality of the ER could cause a state called “ER stress”, which is a hallmark feature of secretory cells and many diseases namely diabetes, neurodegeneration and cancer.
A study lead by Cubillos-Ruiz et al, from Weill Cornell Medical College, New York have proposed a mechanism by which XBP1, a stress sensor of ER can control anti-tumor immunity by disrobing the dentritic cell (DC) homeostasis. Their work was published in Cell, May 2015.
To deal with the protein-folding stress often called the unfolded protein response (UPR), an integrated signal transduction pathway is triggered, and three distinct sensors on the ER membrane are stimulated: IRE1a, ATF6 and PERK. IRE1a, a kinase and being the most conserved arm of the UPR oligomerizes, autophosphorylates, and uses its endoribonuclease activity to excise a 26-nucleotide fragment from the…
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