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@ARTICLE{Brenner:139838,
author = {Brenner, David and Yilmaz, Rüstem and Müller, Kathrin and
Grehl, Torsten and Petri, Susanne and Meyer, Thomas and
Grosskreutz, Julian and Weydt, Patrick and Ruf, Wolfgang and
Neuwirth, Christoph and Weber, Markus and Pinto, Susana and
Claeys, Kristl G and Schrank, Berthold and Jordan, Berit and
Knehr, Antje and Günther, Kornelia and Hübers, Annemarie
and Zeller, Daniel and Kubisch, Christian and Jablonka,
Sibylle and Sendtner, Michael and Klopstock, Thomas and de
Carvalho, Mamede and Sperfeld, Anne and Borck, Guntram and
Volk, Alexander E and Dorst, Johannes and Weis, Joachim and
Otto, Markus and Schuster, Joachim and Del Tredici, Kelly
and Braak, Heiko and Danzer, Karin M and Freischmidt,
Axel-Dieter and Meitinger, Thomas and Strom, Tim M and
Ludolph, Albert and Andersen, Peter M and Weishaupt, Jochen
H and MND-NET, German ALS network and Weyen, Ute and
Hermann, Andreas and Hagenacker, Tim and Koch, Jan Christoph
and Lingor, Paul and Göricke, Bettina and Zierz, Stephan
and Baum, Petra and Wolf, Joachim and Winkler, Andrea and
Young, Peter and Bogdahn, Ulrich and Prudlo, Johannes and
Kassubek, Jan},
title = {{H}ot-spot {KIF}5{A} mutations cause familial {ALS}.},
journal = {Brain},
volume = {141},
number = {3},
issn = {0006-8950},
address = {Oxford},
publisher = {Oxford Univ. Press},
reportid = {DZNE-2020-06160},
pages = {688-697},
year = {2018},
abstract = {Heterozygous missense mutations in the N-terminal motor or
coiled-coil domains of the kinesin family member 5A (KIF5A)
gene cause monogenic spastic paraplegia (HSP10) and
Charcot-Marie-Tooth disease type 2 (CMT2). Moreover,
heterozygous de novo frame-shift mutations in the C-terminal
domain of KIF5A are associated with neonatal intractable
myoclonus, a neurodevelopmental syndrome. These findings,
together with the observation that many of the disease genes
associated with amyotrophic lateral sclerosis disrupt
cytoskeletal function and intracellular transport, led us to
hypothesize that mutations in KIF5A are also a cause of
amyotrophic lateral sclerosis. Using whole exome sequencing
followed by rare variant analysis of 426 patients with
familial amyotrophic lateral sclerosis and 6137 control
subjects, we detected an enrichment of KIF5A splice-site
mutations in amyotrophic lateral sclerosis (2/426 compared
to 0/6137 in controls; P = 4.2 × 10-3), both located in a
hot-spot in the C-terminus of the protein and predicted to
affect splicing exon 27. We additionally show co-segregation
with amyotrophic lateral sclerosis of two canonical
splice-site mutations in two families. Investigation of
lymphoblast cell lines from patients with KIF5A splice-site
mutations revealed the loss of mutant RNA expression and
suggested haploinsufficiency as the most probable underlying
molecular mechanism. Furthermore, mRNA sequencing of a rare
non-synonymous missense mutation (predicting p.Arg1007Gly)
located in the C-terminus of the protein shortly upstream of
the splice donor of exon 27 revealed defective KIF5A
pre-mRNA splicing in respective patient-derived cell lines
owing to abrogation of the donor site. Finally, the
non-synonymous single nucleotide variant rs113247976 (minor
allele frequency = $1.00\%$ in controls, n = 6137), also
located in the C-terminal region [p.(Pro986Leu) in exon 26],
was significantly enriched in familial amyotrophic lateral
sclerosis patients (minor allele frequency = $3.40\%;$ P =
1.28 × 10-7). Our study demonstrates that mutations located
specifically in a C-terminal hotspot of KIF5A can cause a
classical amyotrophic lateral sclerosis phenotype, and
underline the involvement of intracellular transport
processes in amyotrophic lateral sclerosis pathogenesis.},
keywords = {Kinesins: genetics / Adult / Aged / Amyotrophic Lateral
Sclerosis: genetics / DNA Mutational Analysis / Family
Health / Female / Genetic Association Studies / Humans /
Kinesin: genetics / Lymphocytes: drug effects / Lymphocytes:
metabolism / Male / Middle Aged / Mutation: genetics / RNA,
Messenger: genetics / RNA, Messenger: metabolism / KIF5A
protein, human (NLM Chemicals) / RNA, Messenger (NLM
Chemicals) / Kinesin (NLM Chemicals)},
cin = {Clinical Dementia Research München},
ddc = {610},
cid = {I:(DE-2719)1111016},
pnm = {344 - Clinical and Health Care Research (POF3-344)},
pid = {G:(DE-HGF)POF3-344},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:29342275},
pmc = {pmc:PMC5837483},
doi = {10.1093/brain/awx370},
url = {https://pub.dzne.de/record/139838},
}