1,193 results found
    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. 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. 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. 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.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker

    Steffen Preissler et al.
    Interdomain linker-mediated oligomerization of the endoplasmic reticulum chaperone protein BiP responds to the unfolded protein burden
    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. Biochemistry and Chemical Biology
    2. Cell Biology

    An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP

    Kevin D Siegenthaler et al.
    Building on previous work (Wang et al., 2014), it is shown that the nucleotide exchange factor of the chaperone BiP (Sil1) unexpectedly facilitates the reduction of oxidized BiP.
    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. Microbiology and Infectious Disease

    BipA exerts temperature-dependent translational control of biofilm-associated colony morphology in Vibrio cholerae

    Teresa del Peso Santos et al.
    Vibrio cholerae uses a conserved ribosome assembly factor to repress biofilm formation at low temperatures.
    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.

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