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lördag 16 juni 2018

UPR (Unfolded portein response) peruskaava ja ja sovellutusta diabeteksen taustosyiden pohdintoihin

https://www.researchgate.net/figure/The-unfolded-protein-response-UPR-Under-homeostatic-conditions-the-chaperone-BiP-is_fig1_232968324

 The unfolded protein response (UPR). Under homeostatic conditions the chaperone BiP is bound to the luminal domain of the transmembrane proteins ATF6, PERK and IRE1, keeping them inactive. Upon accumulation of unfolded proteins in the ER lumen BiP preferentially binds to them in an attempt to refold these proteins. This allows activation of the three branches of the UPR. (1) ATF6 translocates to the Golgi where it is cleaved by the proteases SP1 and SP2. The fragment generated, ATF6(f), is a transcription factor that modulates the expression of chaperones and enzymes required for ER function. (2) The activation of PERK by autophosphorylation leads to the phosphorylation and inactivation of eIF2 α . eIF2 α is a key initiator of protein translation, and its phosphorylation inhibits global protein translation, decreasing the load on the ER. Paradoxically, translation of some mRNAs such as ATF4 is upregulated. ATF4 
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