NEMO reshapes the α-Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62.
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ABSTRACT:
SUBMITTER: Furthmann N
PROVIDER: S-EPMC10730909 | biostudies-literature | 2023 Dec
REPOSITORIES: biostudies-literature
Publications
NEMO reshapes the α-Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62.
Furthmann Nikolas N Bader Verian V Angersbach Lena L Blusch Alina A Goel Simran S Sánchez-Vicente Ana A Krause Laura J LJ Chaban Sarah A SA Grover Prerna P Trinkaus Victoria A VA van Well Eva M EM Jaugstetter Maximilian M Tschulik Kristina K Damgaard Rune Busk RB Saft Carsten C Ellrichmann Gisa G Gold Ralf R Koch Arend A Englert Benjamin B Westenberger Ana A Klein Christine C Jungbluth Lisa L Sachse Carsten C Behrends Christian C Glatzel Markus M Hartl F Ulrich FU Nakamura Ken K Christine Chadwick W CW Huang Eric J EJ Tatzelt Jörg J Winklhofer Konstanze F KF
Nature communications 20231219 1
NEMO is a ubiquitin-binding protein which regulates canonical NF-κB pathway activation in innate immune signaling, cell death regulation and host-pathogen interactions. Here we identify an NF-κB-independent function of NEMO in proteostasis regulation by promoting autophagosomal clearance of protein aggregates. NEMO-deficient cells accumulate misfolded proteins upon proteotoxic stress and are vulnerable to proteostasis challenges. Moreover, a patient with a mutation in the NEMO-encoding IKBKG gen ...[more]
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