000139838 001__ 139838 000139838 005__ 20240321220708.0 000139838 0247_ $$2doi$$a10.1093/brain/awx370 000139838 0247_ $$2pmid$$apmid:29342275 000139838 0247_ $$2pmc$$apmc:PMC5837483 000139838 0247_ $$2ISSN$$a0006-8950 000139838 0247_ $$2ISSN$$a1460-2156 000139838 0247_ $$2altmetric$$aaltmetric:31582036 000139838 037__ $$aDZNE-2020-06160 000139838 041__ $$aEnglish 000139838 082__ $$a610 000139838 1001_ $$aBrenner, David$$b0 000139838 245__ $$aHot-spot KIF5A mutations cause familial ALS. 000139838 260__ $$aOxford$$bOxford Univ. Press$$c2018 000139838 264_1 $$2Crossref$$3online$$bOxford University Press (OUP)$$c2018-01-12 000139838 264_1 $$2Crossref$$3print$$bOxford University Press (OUP)$$c2018-03-01 000139838 3367_ $$2DRIVER$$aarticle 000139838 3367_ $$2DataCite$$aOutput Types/Journal article 000139838 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1631197322_23921 000139838 3367_ $$2BibTeX$$aARTICLE 000139838 3367_ $$2ORCID$$aJOURNAL_ARTICLE 000139838 3367_ $$00$$2EndNote$$aJournal Article 000139838 520__ $$aHeterozygous 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. 000139838 536__ $$0G:(DE-HGF)POF3-344$$a344 - Clinical and Health Care Research (POF3-344)$$cPOF3-344$$fPOF III$$x0 000139838 542__ $$2Crossref$$i2018-01-12$$uhttp://creativecommons.org/licenses/by-nc/4.0/ 000139838 588__ $$aDataset connected to CrossRef, PubMed, 000139838 650_7 $$2NLM Chemicals$$aKIF5A protein, human 000139838 650_7 $$2NLM Chemicals$$aRNA, Messenger 000139838 650_7 $$0EC 3.6.4.4$$2NLM Chemicals$$aKinesin 000139838 650_2 $$2MeSH$$aKinesins: genetics 000139838 650_2 $$2MeSH$$aAdult 000139838 650_2 $$2MeSH$$aAged 000139838 650_2 $$2MeSH$$aAmyotrophic Lateral Sclerosis: genetics 000139838 650_2 $$2MeSH$$aDNA Mutational Analysis 000139838 650_2 $$2MeSH$$aFamily Health 000139838 650_2 $$2MeSH$$aFemale 000139838 650_2 $$2MeSH$$aGenetic Association Studies 000139838 650_2 $$2MeSH$$aHumans 000139838 650_2 $$2MeSH$$aKinesin: genetics 000139838 650_2 $$2MeSH$$aLymphocytes: drug effects 000139838 650_2 $$2MeSH$$aLymphocytes: metabolism 000139838 650_2 $$2MeSH$$aMale 000139838 650_2 $$2MeSH$$aMiddle Aged 000139838 650_2 $$2MeSH$$aMutation: genetics 000139838 650_2 $$2MeSH$$aRNA, Messenger: genetics 000139838 650_2 $$2MeSH$$aRNA, Messenger: metabolism 000139838 7001_ $$aYilmaz, Rüstem$$b1 000139838 7001_ $$aMüller, Kathrin$$b2 000139838 7001_ $$aGrehl, Torsten$$b3 000139838 7001_ $$aPetri, Susanne$$b4 000139838 7001_ $$aMeyer, Thomas$$b5 000139838 7001_ $$aGrosskreutz, Julian$$b6 000139838 7001_ $$0P:(DE-HGF)0$$aWeydt, Patrick$$b7 000139838 7001_ $$0P:(DE-2719)9001522$$aRuf, Wolfgang$$b8$$udzne 000139838 7001_ $$aNeuwirth, Christoph$$b9 000139838 7001_ $$aWeber, Markus$$b10 000139838 7001_ $$aPinto, Susana$$b11 000139838 7001_ $$aClaeys, Kristl G$$b12 000139838 7001_ $$aSchrank, Berthold$$b13 000139838 7001_ $$aJordan, Berit$$b14 000139838 7001_ $$aKnehr, Antje$$b15 000139838 7001_ $$aGünther, Kornelia$$b16 000139838 7001_ $$0P:(DE-HGF)0$$aHübers, Annemarie$$b17 000139838 7001_ $$aZeller, Daniel$$b18 000139838 7001_ $$aKubisch, Christian$$b19 000139838 7001_ $$aJablonka, Sibylle$$b20 000139838 7001_ $$aSendtner, Michael$$b21 000139838 7001_ $$0P:(DE-2719)2810704$$aKlopstock, Thomas$$b22 000139838 7001_ $$ade Carvalho, Mamede$$b23 000139838 7001_ $$aSperfeld, Anne$$b24 000139838 7001_ $$aBorck, Guntram$$b25 000139838 7001_ $$aVolk, Alexander E$$b26 000139838 7001_ $$aDorst, Johannes$$b27 000139838 7001_ $$aWeis, Joachim$$b28 000139838 7001_ $$aOtto, Markus$$b29 000139838 7001_ $$aSchuster, Joachim$$b30 000139838 7001_ $$aDel Tredici, Kelly$$b31 000139838 7001_ $$aBraak, Heiko$$b32 000139838 7001_ $$0P:(DE-2719)9001513$$aDanzer, Karin M$$b33$$udzne 000139838 7001_ $$0P:(DE-2719)9001054$$aFreischmidt, Axel-Dieter$$b34$$udzne 000139838 7001_ $$0P:(DE-2719)9000207$$aMeitinger, Thomas$$b35$$udzne 000139838 7001_ $$aStrom, Tim M$$b36 000139838 7001_ $$0P:(DE-2719)2812633$$aLudolph, Albert$$b37$$udzne 000139838 7001_ $$aAndersen, Peter M$$b38 000139838 7001_ $$0P:(DE-2719)9000455$$aWeishaupt, Jochen H$$b39$$eCorresponding author$$udzne 000139838 7001_ $$aMND-NET, German ALS network$$b40 000139838 7001_ $$aWeyen, Ute$$b41 000139838 7001_ $$0P:(DE-2719)2811732$$aHermann, Andreas$$b42$$udzne 000139838 7001_ $$aHagenacker, Tim$$b43 000139838 7001_ $$aKoch, Jan Christoph$$b44 000139838 7001_ $$0P:(DE-2719)2812561$$aLingor, Paul$$b45$$udzne 000139838 7001_ $$aGöricke, Bettina$$b46 000139838 7001_ $$aZierz, Stephan$$b47 000139838 7001_ $$aBaum, Petra$$b48 000139838 7001_ $$aWolf, Joachim$$b49 000139838 7001_ $$aWinkler, Andrea$$b50 000139838 7001_ $$aYoung, Peter$$b51 000139838 7001_ $$aBogdahn, Ulrich$$b52 000139838 7001_ $$0P:(DE-2719)2380559$$aPrudlo, Johannes$$b53$$udzne 000139838 7001_ $$aKassubek, Jan$$b54 000139838 77318 $$2Crossref$$3journal-article$$a10.1093/brain/awx370$$b : Oxford University Press (OUP), 2018-01-12$$n3$$p688-697$$tBrain$$v141$$x0006-8950$$y2018 000139838 773__ $$0PERI:(DE-600)1474117-9$$a10.1093/brain/awx370$$gVol. 141, no. 3, p. 688 - 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