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@ARTICLE{Brenner:268729,
author = {Brenner, David and Sieverding, Kirsten and Srinidhi,
Jahnavi and Zellner, Susanne and Secker, Christopher and
Yilmaz, Rüstem and Dyckow, Julia and Amr, Shady and
Ponomarenko, Anna and Tunaboylu, Esra and Douahem, Yasmin
and Schlag, Joana S and Rodriguez Martinez, Lucia and
Kislinger, Georg and Niemann, Cornelia and Nalbach, Karsten
and Ruf, Wolfgang P and Uhl, Jonathan and Hollenbeck,
Johanna and Schirmer, Lucas and Catanese, Alberto and
Lobsiger, Christian S and Danzer, Karin M and
Yilmazer-Hanke, Deniz and Münch, Christian and Koch,
Philipp and Freischmidt, Axel-Dieter and Fetting, Martina
and Behrends, Christian and Parlato, Rosanna and Weishaupt,
Jochen H},
title = {{A} {TBK}1 variant causes autophagolysosomal and motoneuron
pathology without neuroinflammation in mice.},
journal = {Journal of experimental medicine},
volume = {221},
number = {5},
issn = {0022-1007},
address = {New York, NY},
publisher = {Rockefeller Univ. Press},
reportid = {DZNE-2024-00305},
pages = {e20221190},
year = {2024},
abstract = {Heterozygous mutations in the TBK1 gene can cause
amyotrophic lateral sclerosis (ALS) and frontotemporal
dementia (FTD). The majority of TBK1-ALS/FTD patients carry
deleterious loss-of-expression mutations, and it is still
unclear which TBK1 function leads to neurodegeneration. We
investigated the impact of the pathogenic TBK1 missense
variant p.E696K, which does not abolish protein expression,
but leads to a selective loss of TBK1 binding to the
autophagy adaptor protein and TBK1 substrate optineurin.
Using organelle-specific proteomics, we found that in a
knock-in mouse model and human iPSC-derived motor neurons,
the p.E696K mutation causes presymptomatic onset of
autophagolysosomal dysfunction in neurons precipitating the
accumulation of damaged lysosomes. This is followed by a
progressive, age-dependent motor neuron disease. Contrary to
the phenotype of mice with full Tbk1 knock-out,
RIPK/TNF-α-dependent hepatic, neuronal necroptosis, and
overt autoinflammation were not detected. Our in vivo
results indicate autophagolysosomal dysfunction as a trigger
for neurodegeneration and a promising therapeutic target in
TBK1-ALS/FTD.},
keywords = {Animals / Humans / Mice / Amyotrophic Lateral Sclerosis:
pathology / Frontotemporal Dementia: genetics /
Frontotemporal Dementia: metabolism / Frontotemporal
Dementia: pathology / Motor Neurons: pathology / Mutation /
Neuroinflammatory Diseases / Phosphorylation / Protein
Serine-Threonine Kinases: genetics / Protein
Serine-Threonine Kinases: metabolism / Protein
Serine-Threonine Kinases (NLM Chemicals) / TBK1 protein,
human (NLM Chemicals) / Tbk1 protein, mouse (NLM Chemicals)},
cin = {AG Simons / AG Misgeld / AG Danzer},
ddc = {610},
cid = {I:(DE-2719)1110008 / I:(DE-2719)1110000-4 /
I:(DE-2719)5000072},
pnm = {351 - Brain Function (POF4-351) / 352 - Disease Mechanisms
(POF4-352)},
pid = {G:(DE-HGF)POF4-351 / G:(DE-HGF)POF4-352},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:38517332},
pmc = {pmc:PMC10959724},
doi = {10.1084/jem.20221190},
url = {https://pub.dzne.de/record/268729},
}