Selected article for: "ER load and ER stress"
Author: Wang, Ran; Moniruzzaman, Md.; Shuffle, Eric; Lourie, Rohan; Hasnain, Sumaira Z
Title: Immune regulation of the unfolded protein response at the mucosal barrier in viral infection
  • Document date: 2018_4_3
    • ID: 07dlf3zw_3
    Snippet: The UPR pathways trigger a complex network of signals via three ER transmembrane stress sensors: inositol-requiring enzyme 1 a/b (IRE1 a/b, also known as ERN1/2), PKR-like ER kinase (PERK) and activating transcription factor 6 (ATF6), depicted schematically in Figure 1 . Under homeostatic condition, the ER luminal domains of these sensor proteins are inactive, due to association with glucose regulating protein 78 (GRP78; also known as BiP). GRP78.....
    Document: The UPR pathways trigger a complex network of signals via three ER transmembrane stress sensors: inositol-requiring enzyme 1 a/b (IRE1 a/b, also known as ERN1/2), PKR-like ER kinase (PERK) and activating transcription factor 6 (ATF6), depicted schematically in Figure 1 . Under homeostatic condition, the ER luminal domains of these sensor proteins are inactive, due to association with glucose regulating protein 78 (GRP78; also known as BiP). GRP78 has a high affinity for misfolded and unfolded proteins: when luminal load of misfolded protein increases, GRP78 is released from the ER stress sensors, which are then free to initiate downstream signalling outside the ER.

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