75 results found
    1. Cell Biology

    The sterol-responsive RNF145 E3 ubiquitin ligase mediates the degradation of HMG-CoA reductase together with gp78 and Hrd1

    Sam A Menzies et al.
    CRISPR/Cas9 genome-wide screens using sterol-sensitive endogenous HMG-CoA reductase (HMGCR) reporter identify the sterol-responsive RNF145 and gp78 as independently responsible for sterol-accelerated degradation of HMGCR, the rate-limiting enzyme of cholesterol biosynthesis.
    1. Cell Biology

    USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation

    Yanfen Liu et al.
    A deubiquitinase antagonizes the activity of an associated E3 ligase to prevent uncontrolled ubiquitination of a degradation machinery protein and thus maintain its functionality in protein quality control at the endoplasmic reticulum.
    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. Cell Biology

    Proinsulin misfolding is an early event in the progression to type 2 diabetes

    Anoop Arunagiri et al.
    Proinsulin misfolding, an established cause of diabetes in patients with INS gene mutations, is now observed in normal human pancreatic islets, and rodents with genetic predisposition to type 2 diabetes.
    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

    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. Cancer Biology
    2. Immunology and Inflammation

    Preclinical murine tumor models: a structural and functional perspective

    Marion V Guerin et al.
    Dissecting structural, cellular and molecular differences between transplanted and spontaneous mouse tumor models, highlighting their relevance for predicting the efficacy of anti-cancer treatments in patients.
    1. Cell Biology

    Misfolded GPI-anchored proteins are escorted through the secretory pathway by ER-derived factors

    Eszter Zavodszky, Ramanujan S Hegde
    ER-resident chaperones and cargo receptors make excursions to the cell surface and endocytic compartments when they accompany misfolded clients to lysosomes for degradation.
    1. Structural Biology and Molecular Biophysics

    Structural basis of ribosomal peptide macrocyclization in plants

    Joel Haywood et al.
    The first crystal structure of an active plant asparaginyl endopeptidase reveals a tetrahedral intermediate state in its active site, which may help to explain why these enzymes have been independently recruited to perform peptide macrocyclization.

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