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    1. Cell Biology

    The Sec61 translocon limits IRE1α signaling during the unfolded protein response

    Arunkumar Sundaram et al.
    Building on previous work (Plumb et al., 2015), it is shown that the Sec61 translocon controls the oligomerization, activation and inactivation of Ire1α during endoplasmic reticulum stress.
    1. Cell Biology

    Ratiometric sensing of BiP-client versus BiP levels by the unfolded protein response determines its signaling amplitude

    Anush Bakunts et al.
    Restoration of endoplasmic reticulum (ER) homeostatis occurs when levels of the key ER resident chaperone BiP exceed those of accumulating ER clients.
    1. Cell Biology

    Unfolded protein response transducer IRE1-mediated signaling independent of XBP1 mRNA splicing is not required for growth and development of medaka fish

    Tokiro Ishikawa et al.
    The unfolded protein response sensor/transducer IRE1-mediated splicing of XBP1 mRNA encoding its active downstream transcription factor to maintain the homeostasis of the endoplasmic reticulum is sufficient for growth and development of medaka fish.
    1. Cell Biology
    2. Genetics and Genomics

    The Mars1 kinase confers photoprotection through signaling in the chloroplast unfolded protein response

    Karina Perlaza et al.
    A genetic screen in a unicellular photosynthetic organism uncovers the first essential signaling component in the chloroplast unfolded protein response that relays information from the chloroplast to the nuclear compartment.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    An unfolded protein-induced conformational switch activates mammalian IRE1

    G Elif Karagöz et al.
    ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.
    1. Cell Biology

    Experimental reconstitution of chronic ER stress in the liver reveals feedback suppression of BiP mRNA expression

    Javier A Gomez, D Thomas Rutkowski
    Feedback mechanisms that contribute to the deactivation of the unfolded protein response lead to the dysregulation of mRNA expression during chronic stress in the liver, including that of the critical endoplasmic reticulum chaperone BiP.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    tRNA ligase structure reveals kinetic competition between non-conventional mRNA splicing and mRNA decay

    Jirka Peschek, Peter Walter
    Interconnected RNA processing mechanisms ensure the fidelity of non-conventional mRNA splicing during the unfolded protein response.
    1. Cell Biology
    2. Neuroscience

    Adaptation to constant light requires Fic-mediated AMPylation of BiP to protect against reversible photoreceptor degeneration

    Andrew T Moehlman et al.
    Tuning of BiP activity by Fic-mediated AMPylation is required for Drosophila photoreceptor plasticity and attenuation of the unfolded protein response.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Engineering ER-stress dependent non-conventional mRNA splicing

    Weihan Li et al.
    Ire1's RNase specificity and its cleavage sites coordination shape the evolutionary specialization of the unfolded protein response.
    1. Cell Biology

    Inadequate BiP availability defines endoplasmic reticulum stress

    Milena Vitale et al.
    The extent of (proteotoxic) endoplasmic reticulum stress, and the ensuing unfolded protein response activation, are commensurate with the extent of the chaperone BiP being sequestered by its client proteins.