873 results found
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein CH1 to initiate ER stress signaling

    Marta Carrara et al.
    The chaperone protein BiP forms complexes with Ire1 and Perk that dissociate when unfolded proteins bind to BiP to activate the unfolded protein response in the ER.
    1. Cell Biology

    Unstructured regions in IRE1α specify BiP-mediated destabilisation of the luminal domain dimer and repression of the UPR

    Niko Amin-Wetzel et al.
    Client protein-driven reversal of endoplasmic reticulum chaperone (BiP) mediated-repression is revealed as a principal component of the regulation of the unfolded protein response transducer IRE1 in cells.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    In vitro FRET analysis of IRE1 and BiP association and dissociation upon endoplasmic reticulum stress

    Megan C Kopp et al.
    Quantitative FRET UPR induction assay is used to measure IRE1 and BIP association and dissociation by a variety of ER misfolded proteins and by an important BiP substrate-binding domain mutant, significantly enhancing the evidence for the allosteric UPR induction model.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Calcium depletion challenges endoplasmic reticulum proteostasis by destabilising BiP-substrate complexes

    Steffen Preissler et al.
    Regulation of the endoplasmic reticulum chaperone BiP by calcium.
    1. Developmental Biology

    Roles of C/EBP class bZip proteins in the growth and cell competition of Rp (‘Minute’) mutants in Drosophila

    Jorge Blanco et al.
    Xrp1 contributes to cell competition as a heterodimer with the Drosophila C/EBP homolog Irbp18 and although rapidly evolving is itself conserved beyond Drosophila.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    AMPylation matches BiP activity to client protein load in the endoplasmic reticulum

    Steffen Preissler et al.
    Attaching a molecule of adenosine mono-phosphate (AMP) to the BiP protein at threonine 518 regulates its chaperone activity in the endoplasmic reticulum.
    1. Structural Biology and Molecular Biophysics

    Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulation

    Lukasz Wieteska et al.
    The molecular chaperone BIP from the endoplasmic reticulum is fine-tuned postranslationally through the thermodynamic and kinetic alterations in its conformational ensemble of functionally and structurally distinct physiological forms.
    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.
    1. Plant Biology

    Phosphoprotein SAK1 is a regulator of acclimation to singlet oxygen in Chlamydomonas reinhardtii

    Setsuko Wakao et al.
    SAK1, a novel cytoplasmic phosphoprotein, is a key intermediate component of the retrograde signaling pathway controlling nuclear gene expression during acclimation of Chlamydomonas cells to singlet oxygen stress.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress

    Jie Wang et al.
    Direct modification by endogenous peroxide of a conserved cysteine in the molecular chaperone BiP decouples its ATPase and peptide-binding activities, allowing for enhanced polypeptide holdase activity during oxidative stress.

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