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Biology subjects

Korner, R.

Publications and source records attributed to Korner, R..

2 recordsLinked to original sources

Virus-mediated tau aggregate seeding in a cellular model

Formation of neuronal tau protein aggregates is a defining feature of tauopathies, including Alzheimers 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 implicated viral infections in aggregate-associated neurodegeneration, the underlying mechanisms remain unclear. Here, we show in a cell culture model that seeding competent tau aggregates are efficiently packaged into lentiviral particles and induce tau aggregation in recipient cells in a virus receptor-dependent manner. Tau aggregates interact with the viral Gag polyprotein, likely facilitating their incorporation into virions. Virus-dependent tau seeding requires protease-mediated maturation of the envelope protein to enable efficient fusion of the viral envelope with the plasma membrane of the recipient cell. Thus, tau aggregate packaging is compatible with the formation of mature, infectious virions. These findings are consistent with a possible role of viral infection in neurodegenerative disease progression and offer a robust, versatile platform to model tau propagation in cellular systems and animal models.

Cell Biology↗

Oligosaccharyltransferase is involved in targeting to ER-associated degradation

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 as key interactors with a misfolded ER protein bait, suggesting unexpected involvement in ERAD. Previous reports implied additional roles for OST subunits beyond N-glycosylation, such as quality control by ribophorin I. We tested OST engagement in glycoprotein and non-glycosylated protein ERAD; overexpression or partial knockdown of OST subunits interfered with ERAD in conditions that did not affect glycosylation. Effects were studied on misfolded membrane proteins, BACE476 and asialoglycoprotein receptor H2a, and the luminal 1-antitrypsin NHK variant. OST appears to participate in late ERAD stages, interacting with the E3 ligase HRD1 and facilitating retrotranslocation. Molecular dynamics simulations suggest membrane thinning by OST transmembrane domains, possibly assisting retrotranslocation via membrane distortion.

cell biology↗