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• W3023144423 abstract "Protein aggregates formed by microtubule-associated protein Tau can be transmitted in a stereotypic pattern in human brains, which correlates with the progression of several neurodegenerative diseases collectively termed Tauopathies. This process requires Tau, released from neurons, to interact with a cell surface receptor on a target cell, but little is known about the underlying mechanisms and the downstream pathophysiological consequences particularly for Tau that engages glial cells. Using a spatially resolved proteomic mapping strategy, we identify integrin αV/β1, a heterodimer of the integrin family, as a receptor that not only mediates Tau fibril entry into astrocytes, but also activates integrin signaling upon Tau binding. We show that distinct Tau species differentially activates integrin signaling, with filamentous Tau being a more robust stimulator. This leads to differential upregulation of pro-inflammatory cytokines and chemokines. Additionally, a sub-group of neurotoxic astrocyte markers are also induced in an integrin-dependent manner preferentially by filamentous Tau, causing astrocytes to release a neurotoxic factor(s). Together, these findings establish a paradigm that astrocytes can be directly converted into a neurotoxic state by filamentous Tau via an integrin receptor, which as a sensor transducing unfolded protein pathology, may provide a new therapeutic target for Tauopathies." @default.
• W3023144423 created "2020-05-13" @default.
• W3023144423 creator A5046551911 @default.
• W3023144423 creator A5049078993 @default.
• W3023144423 date "2020-05-10" @default.
• W3023144423 modified "2023-09-23" @default.
• W3023144423 title "An integrin receptor complex mediates filamentous Tau-induced activation of primary astrocytes" @default.
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