CRISPR screens in iPSC-derived neurons reveal principles of tau proteostasis
Avi J. Samelson(University of California, Los Angeles), Nabeela Ariqat(University of California, San Francisco), Justin McKetney(QB3), Gita Rohanitazangi(University of California, San Francisco), C Bravo(Cornell University), Rudra Shekhar Bose(University of California, San Francisco), Kyle J. Travaglini(Allen Institute for Brain Science), Victor L. Lam(University of California, San Francisco), Darrin Goodness(University of California, San Francisco), Thomas Ta(University of California, San Francisco), Gary Dixon(University of California, San Francisco), Emily Marzette(University of California, San Francisco), Julianne Jin(University of California, San Francisco), Ruilin Tian(University of California, San Francisco), Eric Tse(University of California, San Francisco), Romany Abskharon(University of California, Los Angeles), Henry S. Pan(University of California, San Francisco), Emma C. Carroll(San Jose State University), Rosalie Lawrence(QB3), Jason E. Gestwicki(University of California, San Francisco), Jessica E. Rexach(University of California, Los Angeles), David Eisenberg(Howard Hughes Medical Institute), Nicholas M. Kanaan(Michigan State University), Daniel R. Southworth(University of California, San Francisco), John D. Gross(University of California, San Francisco), Li Gan(Cornell University), Danielle L. Swaney(QB3), Martin Kampmann(University of California, San Francisco)
Cited by 8Open Access
Abstract
controls tau levels in human neurons, ubiquitinates tau, and is correlated with resilience to tauopathies in human disease. Disruption of mitochondrial function promotes proteasomal misprocessing of tau, generating disease-relevant tau proteolytic fragments and changing tau aggregation in vitro. These results systematically reveal principles of tau proteostasis in human neurons and suggest potential therapeutic targets for tauopathies.
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