Roman Körner

Virus-mediated tau aggregate seeding in a cellular model

Patricia Yuste‐Checa, Roman D Martinez-Piera, Freya Herrmann-Sim, L. Sofia Ronquillo-Silva et autres

Abstract Formation of neuronal tau protein aggregates is a defining feature of tauopathies, including Alzheimer’s disease and frontotemporal dementia. Tau pathology propagates across brain regions by a cell-to-cell aggregate seeding mechanism. While epidemiological and experimental studies over the past three decades have …

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Oligosaccharyltransferase Is Involved in Targeting to ER-Associated Degradation

Marina Shenkman, Navit Ogen‐Shtern, Chaitanya Patel, Haddas Saad et autres

Most membrane and secretory proteins undergo N-glycosylation, catalyzed by oligosaccharyltransferase (OST), a membrane-bound complex in the endoplasmic reticulum (ER). Proteins failing quality control are degraded via ER-associated degradation (ERAD), involving retrotranslocation to cytosolic proteasomes, or relegated to ER subdomains and eliminated via …

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Mitochondrial proteostatic stress disrupts mitoribosome biogenesis and translation

Hauke Holthusen, Victoria A. Trinkaus, Carina Fernandez Gonzalez, Itika Saha et autres

SUMMARY Protein aggregation in various cellular compartments is a hallmark of proteostasis impairment linked to aging and numerous pathologies. Mitochondrial function depends on a balanced interplay of proteins imported from the cytosol as well as those synthesized on mitochondrial ribosomes (mitoribosomes). Here, …

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Visualizing chaperonin function in situ by cryo-electron tomography

Jonathan Wagner, Alonso I. Carvajal, Andreas Bracher, Florian Beck et autres

Abstract Chaperonins are large barrel-shaped complexes that mediate ATP-dependent protein folding1–3. The bacterial chaperonin GroEL forms juxtaposed rings that bind unfolded protein and the lid-shaped cofactor GroES at their apertures. In vitro analyses of the chaperonin reaction have shown that substrate protein …

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Oligosaccharyltransferase is involved in targeting to ER-associated degradation

Marina Shenkman, Navit Ogen‐Shtern, Chaitanya Patel, Bella Groisman et autres

Abstract Most membrane and secretory proteins undergo N-glycosylation, catalyzed by oligosaccharyltransferase (OST), a membrane-bound complex in the endoplasmic reticulum (ER). Proteins failing quality control are degraded via ER-associated degradation (ERAD), involving retrotranslocation to cytosolic proteasomes. Using SILAC proteomics, we identified OST subunits …

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The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds in a cellular system

Itika Saha, Patricia Yuste‐Checa, Miguel da Silva Padilha, Qiang Guo et autres

Amyloid-like aggregates of the microtubule-associated protein Tau are associated with several neurodegenerative disorders including Alzheimer's disease. The existence of cellular machinery for the removal of such aggregates has remained unclear, as specialized disaggregase chaperones are thought to be absent in mammalian cells. …

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The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds

Itika Saha, Patricia Yuste‐Checa, Miguel da Silva Padilha, Qiang Guo et autres

Abstract Amyloid-like aggregates of the microtubule-associated protein Tau are associated with several neurodegenerative disorders including Alzheimer’s disease. The existence of cellular machinery for the removal of such aggregates has remained unclear, as specialized disaggregase chaperones are thought to be absent in mammalian …

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An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space

Anne Sigaard Bie, Cagla Cömert, Roman Körner, Thomas J. Corydon et autres

The HSP60/HSP10 chaperonin assists folding of proteins in the mitochondrial matrix space by enclosing them in its central cavity. The chaperonin forms part of the mitochondrial protein quality control system. It is essential for cellular survival and mutations in its subunits are …

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The nucleolus functions as a phase-separated protein quality control compartment

Frédéric Frottin, Florian Schueder, Shivani Tiwary, Rajat M. Gupta et autres

The nuclear proteome is rich in stress-sensitive proteins, which suggests that effective protein quality control mechanisms are in place to ensure conformational maintenance. We investigated the role of the nucleolus in this process. In mammalian tissue culture cells under stress conditions, misfolded …

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The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli

Liang Zhao, Giulia Vecchi, Michele Vendruscolo, Roman Körner et autres

Stress-inducible molecular chaperones have essential roles in maintaining protein homeostasis, but the extent to which they affect overall proteome stability remains unclear. Here, we analyze the effects of the DnaK (Hsp70) system on protein stability in Escherichia coli using pulse proteolysis combined …

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Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2

Leonie Mönkemeyer, Courtney L. Klaips, David Balchin, Roman Körner et autres

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Proteome-wide analysis of protein stability in E. coli using pulse proteolysis

Liang Zhao, Giulia Vecchi, Michele Vendruscolo, Roman Körner et autres

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