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Автор: Grafiati

Опубліковано: 11 вересня 2023

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1

Rahman, Amena, Adeela Kamal, Elizabeth A. Roberts, and Lawrence S. B. Goldstein. "Defective Kinesin Heavy Chain Behavior in Mouse Kinesin Light Chain Mutants." Journal of Cell Biology 146, no. 6 (September 20, 1999): 1277–88. http://dx.doi.org/10.1083/jcb.146.6.1277.

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Анотація:

Conventional kinesin, kinesin-I, is a heterotetramer of two kinesin heavy chain (KHC) subunits (KIF5A, KIF5B, or KIF5C) and two kinesin light chain (KLC) subunits. While KHC contains the motor activity, the role of KLC remains unknown. It has been suggested that KLC is involved in either modulation of KHC activity or in cargo binding. Previously, we characterized KLC genes in mouse (Rahman, A., D.S. Friedman, and L.S. Goldstein. 1998. J. Biol. Chem. 273:15395–15403). Of the two characterized gene products, KLC1 was predominant in neuronal tissues, whereas KLC2 showed a more ubiquitous pattern of expression. To define the in vivo role of KLC, we generated KLC1 gene-targeted mice. Removal of functional KLC1 resulted in significantly smaller mutant mice that also exhibited pronounced motor disabilities. Biochemical analyses demonstrated that KLC1 mutant mice have a pool of KIF5A not associated with any known KLC subunit. Immunofluorescence studies of sensory and motor neuron cell bodies in KLC1 mutants revealed that KIF5A colocalized aberrantly with the peripheral cis-Golgi marker giantin in mutant cells. Striking changes and aberrant colocalization were also observed in the intracellular distribution of KIF5B and β′-COP, a component of COP1 coatomer. Taken together, these data best support models that suggest that KLC1 is essential for proper KHC activation or targeting.

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2

Kanai, Yoshimitsu, Yasushi Okada, Yousuke Tanaka, and Nobutaka Hirokawa. "605 Localization of kinesin heavy chains (KIF5A, KIF5B, KIF5C) in nervous system." Neuroscience Research 28 (January 1997): S84. http://dx.doi.org/10.1016/s0168-0102(97)90217-0.

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3

Tian, Da-Wei, Zhou-Liang Wu, Li-Ming Jiang, Jie Gao, Chang-Li Wu, and Hai-Long Hu. "KIF5A Promotes Bladder Cancer Proliferation In Vitro and In Vivo." Disease Markers 2019 (July 3, 2019): 1–9. http://dx.doi.org/10.1155/2019/4824902.

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Background. Bladder cancer is a common malignancy with uncontrolled and rapid growth. Although lots of the important regulatory networks in bladder cancer have been found, the cancer-relevant genes remain to be further identified. Methods. We examined the KIF5A expression levels in bladder cancer and normal bladder tissue samples via immunohistochemistry and observed the effect of KIF5A on bladder tumor cell proliferation in vitro and in vivo. Additionally, a coexpression between KIF5A and KIF20B in tumor tissues was explored. Results. KIF5A expression level was higher in the bladder cancer tissues than in the adjacent nontumor tissues. Patients with higher KIF5A expression displayed advanced clinical features and shorter survival time than those with lower KIF5A expression. Moreover, KIF5A knockdown inhibited bladder cancer cell proliferation, migration, and invasion demonstrated in vivo and in vitro. In addition, coexpression was found between KIF5A and KIF20B in tumor tissues. Conclusion. The results demonstrated that KIF5A is a critical regulator in bladder cancer development and progression, as well as a potential target in the treatment of bladder cancer.

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4

Hares, Kelly, Scott Miners, Neil Scolding, Seth Love, and Alastair Wilkins. "KIF5A and KLC1 expression in Alzheimer’s disease: relationship and genetic influences." AMRC Open Research 1 (June 26, 2019): 1. http://dx.doi.org/10.12688/amrcopenres.12861.2.

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Background: Early disturbances in axonal transport, before the onset of gross neuropathology, occur in a spectrum of neurodegenerative diseases including Alzheimer’s disease. Kinesin superfamily motor proteins (KIFs) are responsible for anterograde protein transport within the axon of various cellular cargoes, including synaptic and structural proteins. Dysregulated KIF expression has been associated with AD pathology and genetic polymorphisms within kinesin-light chain-1 (KLC1) have been linked to AD susceptibility. We examined the expression of KLC1 in AD, in relation to that of the KLC1 motor complex (KIF5A) and to susceptibility genotypes. Methods: We analysed KLC1 and KIF5A gene and protein expression in midfrontal cortex from 47 AD and 39 control brains. Results: We found that gene expression of both KIF5A and KLC1 increased with Braak tangle stage (0-II vs III-IV and V-VI) but was not associated with significant change at the protein level. We found no effect of KLC1 SNPs on KIF5A or KLC1 expression but KIF5A SNPs that had previously been linked to susceptibility in multiple sclerosis were associated with reduced KIF5A mRNA expression in AD cortex. Conclusions: Future in vitro and in vivo studies are required to understand the cause of upregulated KIF5A and KLC-1 gene expression in AD and any potential downstream consequences on pathogenesis, including any contribution of genetic polymorphisms within the KIF5A gene locus.

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5

Hares, Kelly, Scott Miners, Neil Scolding, Seth Love, and Alastair Wilkins. "KIF5A and KLC1 expression in Alzheimer’s disease: relationship and genetic influences." AMRC Open Research 1 (February 19, 2019): 1. http://dx.doi.org/10.12688/amrcopenres.12861.1.

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Анотація:

Background: Early disturbances in axonal transport, before the onset of gross neuropathology, occur in a spectrum of neurodegenerative diseases including Alzheimer’s disease. Kinesin superfamily motor proteins (KIFs) are responsible for anterograde protein transport within the axon of various cellular cargoes, including synaptic and structural proteins. Dysregulated KIF expression has been associated with AD pathology and genetic polymorphisms within kinesin-light chain-1 (KLC1) have been linked to AD susceptibility. We examined the expression of KLC1 in AD, in relation to that of the KLC1 motor complex (KIF5A) and to susceptibility genotypes. Methods: We analysed KLC1 and KIF5A gene and protein expression in midfrontal cortex from 47 AD and 39 control brains. Results: We found that gene expression of both KIF5A and KLC1 increased with Braak tangle stage (0-II vs III-IV and V-VI) but was not associated with significant change at the protein level. We found no effect of KLC1 SNPs on KIF5A or KLC1 expression but KIF5A SNPs that had previously been linked to susceptibility in multiple sclerosis were associated with reduced KIF5A mRNA expression in AD cortex. Conclusions: The findings raise the possibility that genetic polymorphisms within the KIF5A gene locus could contribute to disturbances of axonal transport, neuronal connectivity and function across a spectrum of neurological conditions, including AD.

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6

Hares, Kelly, K. Kemp, S. Loveless, C. M. Rice, N. Scolding, E. Tallantyre, N. Robertson, and A. Wilkins. "KIF5A and the contribution of susceptibility genotypes as a predictive biomarker for multiple sclerosis." Journal of Neurology 268, no. 6 (January 23, 2021): 2175–84. http://dx.doi.org/10.1007/s00415-020-10373-w.

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AbstractThere is increasing interest in the development of multiple sclerosis (MS) biomarkers that reflect central nervous system tissue injury to determine prognosis. We aimed to assess the prognostic value of kinesin superfamily motor protein KIF5A in MS by measuring levels of KIF5A in cerebrospinal fluid (CSF) combined with analysis of single nucleotide polymorphisms (SNPs; rs12368653 and rs703842) located within a MS susceptibility gene locus at chromosome 12q13–14 region. Enzyme-linked immunosorbent assay was used to measure KIF5A in CSF obtained from two independent biobanks comprising non-inflammatory neurological disease controls (NINDC), clinically isolated syndrome (CIS) and MS cases. CSF KIF5A expression was significantly elevated in progressive MS cases compared with NINDCs, CIS and relapsing–remitting MS (RRMS). In addition, levels of KIF5A positively correlated with change in MS disease severity scores (EDSS, MSSS and ARMSSS), in RRMS patients who had documented disease progression at 2-year clinical follow-up. Copies of adenine risk alleles (AG/AA; rs12368653 and rs703842) corresponded with a higher proportion of individuals in relapse at the time of lumbar puncture (LP), higher use of disease-modifying therapies post LP and shorter MS duration. Our study suggests that CSF KIF5A has potential as a predictive biomarker in MS and further studies into the potential prognostic value of analysing MS susceptibility SNPs should be considered.

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7

Mahase, Vidhyanand, Adebiyi Sobitan, Christina Johnson, Farion Cooper, Yixin Xie, Lin Li, and Shaolei Teng. "Computational analysis of hereditary spastic paraplegia mutations in the kinesin motor domains of KIF1A and KIF5A." Journal of Theoretical and Computational Chemistry 19, no. 06 (August 5, 2020): 2041003. http://dx.doi.org/10.1142/s0219633620410035.

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Hereditary spastic paraplegias (HSPs) are a genetically heterogeneous collection of neurodegenerative disorders categorized by progressive lower-limb spasticity and frailty. The complex HSP forms are characterized by various neurological features including progressive spastic weakness, urinary sphincter dysfunction, extra pyramidal signs and intellectual disability (ID). The kinesin superfamily proteins (KIFs) are microtubule-dependent molecular motors involved in intracellular transport. Kinesins directionally transport membrane vesicles, protein complexes, and mRNAs along neurites, thus playing important roles in neuronal development and function. Recent genetic studies have identified kinesin mutations in patients with HSPs. In this study, we used the computational approaches to investigate the 40 missense mutations associated with HSP and ID in KIF1A and KIF5A. We performed homology modeling to construct the structures of kinesin–microtubule binding domain and kinesin–tubulin complex. We applied structure-based energy calculation methods to determine the effects of missense mutations on protein stability and protein–protein interaction. The results revealed that the most of disease-causing mutations could change the folding free energy of kinesin motor domain and the binding free energy of kinesin–tubulin complex. We found that E253K associated with ID in KIF1A decrease the protein stability of kinesin motor domains. We showed that the HSP mutations located in kinesin–tubulin complex interface, such as K253N and R280C in KIF5A, can destabilize the kinesin–tubulin complex. The computational analysis provides useful information for understanding the roles of kinesin mutations in the development of ID and HSPs.

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8

KALCHISHKOVA, NIKOLINA, and KONRAD J. BÖHM. "ON THE RELEVANCE OF THE CORE HELIX ALPHA 6 TO KINESIN ACTIVITY GENERATION." Biophysical Reviews and Letters 04, no. 01n02 (April 2009): 63–75. http://dx.doi.org/10.1142/s1793048009000934.

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KIF5A and Eg5 are plus-end directed motor proteins with conserved motor domains. The catalytic cores of both motors comprise a central β-sheet consisting of eight β-strands surrounded by six α-helices. Notwithstanding the high level of similarity in their structural organization, Eg5 moves significantly slower than KIF5A. Recently, we reported that neck linker and neck elements of KIF5A and Eg5 contribute to velocity regulation. As the neck linker of both motors is known to be connected to the catalytic core via helix α6, the question arises if also helix α6 and strand β8 as the last core elements might be involved in velocity regulation. To elucidate the role these structures in kinesin activity generation we constructed KIF5A- and Eg5-based chimeras in which the β8 strand, helix α6, the neck linker, and the neck were interchanged. Additionally, we studied the role of α6 and β8 in ATP hydrolysis and microtubule binding by expression of truncated KIF5A and Eg5 constructs lacking both strand β8 and helix α6, or α6 only. The results obtained suggest that strand β8 and helix α6 are not involved in microtubule-binding, but α6 is an obligate and kinesin type-specific structure required to generate ATPase activity.

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9

Filosto, Massimiliano, Stefano Piccinelli, Ilaria Palmieri, Nicola Necchini, Marialuisa Valente, Isabella Zanella, Giorgio Biasiotto, Diego Lorenzo, Cristina Cereda, and Alessandro Padovani. "A Novel Mutation in the Stalk Domain of KIF5A Causes a Slowly Progressive Atypical Motor Syndrome." Journal of Clinical Medicine 8, no. 1 (December 22, 2018): 17. http://dx.doi.org/10.3390/jcm8010017.

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KIF5A encodes the heavy chain A of kinesin; A motor protein involved in motility functions within neuron. Mutations in the KIF5A N-terminal motor domain are known to cause SPG10; An autosomal dominant hereditary spastic paraplegia (HSP), as well as rare Charcot-Marie-Tooth disease 2 (CMT2) cases. Recently C-terminal cargo-binding tail domain mutations have been associated with an amyotrophic lateral sclerosis (ALS) phenotype. Here we describe a subject presenting with an atypical slowly progressive motor syndrome evolving over a period of 4 years; Characterized by walking difficulties; Muscle hypotrophy mainly involving upper limbs and pyramidal signs confined to the lower limbs. Electromyography demonstrated chronic neurogenic damage and active denervation while electroneurography showed slowly worsening axonal damage. We identified the novel heterozygote variant c.2341A>G in the exon 21 of the KIF5A gene resulting in the amino acid change p.Lys781Glu. The residue Lys781 is located within the terminal region of the stalk domain and is highly evolutionary conserved. Our findings confirm that mutations in KIF5A cause ALS-like phenotypes. However, the stalk domain mutation described here appears to result in an “intermediate” slowly progressive phenotype having aspects resembling ALS as well as HSP and axonal neuropathy. We suggest that KIF5A gene should be considered as a candidate gene in all atypical progressive motor syndromes.

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10

Nakajima, Kazuo, Xiling Yin, Yosuke Takei, Dae-Hyun Seog, Noriko Homma, and Nobutaka Hirokawa. "Molecular Motor KIF5A Is Essential for GABAA Receptor Transport, and KIF5A Deletion Causes Epilepsy." Neuron 76, no. 5 (December 2012): 945–61. http://dx.doi.org/10.1016/j.neuron.2012.10.012.

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11

Hares, K., K. Kemp, C. Rice, E. Gray, N. Scolding, and A. Wilkins. "Reduced axonal motor protein expression in non-lesional grey matter in multiple sclerosis." Multiple Sclerosis Journal 20, no. 7 (October 21, 2013): 812–21. http://dx.doi.org/10.1177/1352458513508836.

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Background: Multiple sclerosis (MS) is a neurological disease characterised by central nervous system inflammation, demyelination, axonal degeneration and neuronal injury. Preventing neuronal and axon damage is of paramount importance in attempts to prevent disease progression. Intact axonal transport mechanisms are crucial to axonal integrity and evidence suggests these mechanisms are disrupted in MS. Anterograde axonal transport is mediated to a large extent through the kinesin superfamily proteins. Recently, certain kinesin superfamily proteins (KIF5A, KIF1B and KIF21B) were implicated in MS pathology. Objectives: To investigate the expression of KIF5A, KIF21B and KIF1B in MS and control post-mortem grey matter. Methods: Using both quantitative real-time polymerase chain reaction (PCR) and Immunodot-blots assays, we analysed the expression of kinesin superfamily proteins in 27 MS cases and 13 control cases not linked to neurological disease. Results: We have shown significant reductions in KIF5A, KIF21B and KIF1B messenger ribonucleic acid (mRNA) expression and also KIF5A protein expression in MS grey matter, as compared to control grey matter. Conclusion: We have shown significant reductions in mRNA and protein levels of axonal motor proteins in the grey matter of MS cases, which may have important implications for the pathogenesis of neuronal/axonal injury in the disease.

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12

Cuchanski, Mathieu, and Kelly Jo Baldwin. "Mutation in KIF5A c.610C>T Causing Hereditary Spastic Paraplegia with Axonal Sensorimotor Neuropathy." Case Reports in Neurology 10, no. 2 (July 4, 2018): 165–68. http://dx.doi.org/10.1159/000490456.

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Hereditary spastic paraplegias (HSP) are a rare heterogeneous group of inherited neurodegenerative diseases characterized by progressive lower extremity spasticity and weakness. Mutations of the kinesin family member 5A (KIF5A) gene lead to a spectrum of phenotypes ranging from spastic paraplegia type 10 to Charcot-Marie Tooth Disease type 2. We report the second known case of a mutation in the KIF5A gene at c.610C>T presenting with HSP plus an axonal sensorimotor neuropathy.

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13

Xia, Chun-Hong, Elizabeth A. Roberts, Lu-Shiun Her, Xinran Liu, David S. Williams, Don W. Cleveland, and Lawrence S. B. Goldstein. "Abnormal neurofilament transport caused by targeted disruption of neuronal kinesin heavy chain KIF5A." Journal of Cell Biology 161, no. 1 (April 7, 2003): 55–66. http://dx.doi.org/10.1083/jcb.200301026.

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To test the hypothesis that fast anterograde molecular motor proteins power the slow axonal transport of neurofilaments (NFs), we used homologous recombination to generate mice lacking the neuronal-specific conventional kinesin heavy chain, KIF5A. Because null KIF5A mutants die immediately after birth, a synapsin-promoted Cre-recombinase transgene was used to direct inactivation of KIF5A in neurons postnatally. Three fourths of such mutant mice exhibited seizures and death at around 3 wk of age; the remaining animals survived to 3 mo or longer. In young mutant animals, fast axonal transport appeared to be intact, but NF-H, as well as NF-M and NF-L, accumulated in the cell bodies of peripheral sensory neurons accompanied by a reduction in sensory axon caliber. Older animals also developed age-dependent sensory neuron degeneration, an accumulation of NF subunits in cell bodies and a reduction in axons, loss of large caliber axons, and hind limb paralysis. These data support the hypothesis that a conventional kinesin plays a role in the microtubule-dependent slow axonal transport of at least one cargo, the NF proteins.

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14

Moe, Aye, Andrew Schaefer, Gráinne Gorman, and Yi Shiau Ng. "Changing phenotypes, a spectrum over 10 years." Journal of Neurology, Neurosurgery & Psychiatry 93, no. 9 (August 12, 2022): e2.189. http://dx.doi.org/10.1136/jnnp-2022-abn2.42.

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Our patient first presented with progressive unsteadiness and slurred speech at the age of 67 years. The initial working diagnosis was progressive ataxia. There were minimal cerebellar changes on MRI head and extensive laboratory tests including common spinocerebellar ataxia screen was negative. He sub- sequently developed distal muscle wasting and weakness, and pathologically brisk reflexes, with normal CK levels. Motor neuron disease (MND) was then clinically suspected, however, further neurophysiologi- cal studies and a nerve biopsy revealed changes consistent with an axonal neuropathy. Generalised muscle wasting, bilateral scapular winging, eyelid ptosis and complex ophthalmoplegia were identified eight years after initial clinic review. The complex evolving neurological phenotype prompted a muscle biopsy to investigate for mitochondrial disease. Whilst some evidence of mitochondrial dysfunction was identified, the mitochondrial DNA maintenance nuclear gene panel was negative. He was enrolled to the 100k genome project which revealed a heterozygous KIF5A pathogenic variant. Mutations in KIF5A are associated with a wide phenotypic spectrum including CMT neuropathy, hereditary spastic paraplegia and MND-like syndrome. Our case highlights the diagnostic conundrum of evolving neurological mani- festations of KIF5A disease that demonstrates overlapping cardinal features with mitochondrial disease.

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15

Brenner, David, Rüstem Yilmaz, Kathrin Müller, Torsten Grehl, Susanne Petri, Thomas Meyer, Julian Grosskreutz, et al. "Hot-spot KIF5A mutations cause familial ALS." Brain 141, no. 3 (January 12, 2018): 688–97. http://dx.doi.org/10.1093/brain/awx370.

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16

CHIBA, Kyoko. "Analysis of ALS-associated Mutant of KIF5A." Seibutsu Butsuri 63, no. 3 (2023): 169–70. http://dx.doi.org/10.2142/biophys.63.169.

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17

Andréasson, Mattias, Kristina Lagerstedt-Robinson, Kristin Samuelsson, Göran Solders, Kaj Blennow, Martin Paucar, and Per Svenningsson. "Altered CSF levels of monoamines in hereditary spastic paraparesis 10." Neurology Genetics 5, no. 4 (June 12, 2019): e344. http://dx.doi.org/10.1212/nxg.0000000000000344.

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ObjectiveTo perform a comprehensive clinical characterization and biochemical CSF profile analyses in 2 Swedish families with hereditary spastic paraparesis (HSP) 10 (SPG10) caused by 2 different mutations in the neuronal kinesin heavy chain gene (KIF5A).MethodsStructured clinical assessment, genetic studies, and neuroradiologic and electrophysiological evaluations were performed in 4 patients from 2 families with SPG10. Additional CSF analysis was conducted in 3 patients with regard to levels of neurodegenerative markers and monoamine metabolism.ResultsAll patients exhibited a complex form of HSP with a mild to moderate concurrent axonal polyneuropathy. The heterozygous missense mutations c.767A>G and c.967C>T in KIF5A were found. Wide intrafamilial phenotype variability was evident in both families. CSF analysis demonstrated a mild elevation of neurofilament light (NFL) chain in the patient with longest disease duration. Unexpectedly, all patients exhibited increased levels of the dopamine metabolite, homovanillic acid, whereas decreased levels of the noradrenergic metabolite, 3-methoxy-4-hydroxyphenylglycol, were found in 2 of 3 patients.ConclusionsWe report on CSF abnormalities in SPG10, demonstrating that NFL elevation is not a mandatory finding but may appear after long-standing disease. Impaired transportation of synaptic proteins may be a possible explanation for the increased dopaminergic turnover and noradrenergic deficiency identified. The reasons for these selective abnormalities, unrelated to obvious clinical features, remain to be explained. Our findings need further confirmation in larger cohorts of patients harboring KIF5A mutations.

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18

Kanai, Yoshimitsu, Yasushi Okada, Yosuke Tanaka, and Nobutaka Hirokawa. "Differential localization of neuronal (KIF5A and KIF 5C) and ubiquitous (KIF5B) kinesin heavy chains in nervous system." Neuroscience Research 31 (January 1998): S132. http://dx.doi.org/10.1016/s0168-0102(98)82022-1.

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19

Karle, Kathrin N., Diana Möckel, Evan Reid, and Ludger Schöls. "Axonal transport deficit in a KIF5A –/– mouse model." neurogenetics 13, no. 2 (April 1, 2012): 169–79. http://dx.doi.org/10.1007/s10048-012-0324-y.

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20

Yang, Tien-Chun, Aliaksandr A. Yarmishyn, Yi-Ping Yang, Pin-Chen Lu, Shih-Jie Chou, Mong-Lien Wang, Tai-Chi Lin, et al. "Mitochondrial transport mediates survival of retinal ganglion cells in affected LHON patients." Human Molecular Genetics 29, no. 9 (April 10, 2020): 1454–64. http://dx.doi.org/10.1093/hmg/ddaa063.

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Abstract The mutations in the genes encoding the subunits of complex I of the mitochondrial electron transport chain are the most common cause of Leber’s hereditary optic neuropathy (LHON), a maternal hereditary disease characterized by retinal ganglion cell (RGC) degeneration. The characteristics of incomplete penetrance indicate that nuclear genetic and environmental factors also determine phenotypic expression of LHON. Therefore, further understanding of the role of mutant mitochondrial nicotinamide adenine dinucleotide dehydrogenase subunit proteins and nuclear genetic factors/environmental effects in the etiology of LHON is needed. In this study, we generated human-induced pluripotent stem cells (hiPSCs) from healthy control, unaffected LHON mutation carrier, and affected LHON patient. hiPSC-derived RGCs were used to study the differences between affected and unaffected carriers of mitochondrial DNA point mutation m.11778G > A in the MT-ND4 gene. We found that both mutated cell lines were characterized by increase in reactive oxygen species production, however, only affected cell line had increased levels of apoptotic cells. We found a significant increase in retrograde mitochondria and a decrease in stationary mitochondria in the affected RGC axons. In addition, the messenger RNA and protein levels of KIF5A in the LHON-affected RGCs were significantly reduced. Antioxidant N-acetyl-L-cysteine could restore the expression of KIF5A and the normal pattern of mitochondrial movement in the affected RGCs. To conclude, we found essential differences in the mutually dependent processes of oxidative stress, mitochondrial transport and apoptosis between two LHON-specific mutation carrier RGC cell lines, asymptomatic carrier and disease-affected, and identified KIF5A as a central modulator of these differences.

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21

Nicolas, Aude, Kevin P. Kenna, Alan E. Renton, Nicola Ticozzi, Faraz Faghri, Ruth Chia, Janice A. Dominov, et al. "Genome-wide Analyses Identify KIF5A as a Novel ALS Gene." Neuron 97, no. 6 (March 2018): 1268–83. http://dx.doi.org/10.1016/j.neuron.2018.02.027.

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22

Zhang, Kang, Qing Liu, Dongchao Shen, Hongfei Tai, Shuangwu Liu, Zhili Wang, Jiayu Shi, et al. "Mutation analysis of KIF5A in Chinese amyotrophic lateral sclerosis patients." Neurobiology of Aging 73 (January 2019): 229.e1–229.e4. http://dx.doi.org/10.1016/j.neurobiolaging.2018.08.006.

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23

Wang, Qi, Jing Tian, Hao Chen, Heng Du, and Lan Guo. "Amyloid beta-mediated KIF5A deficiency disrupts anterograde axonal mitochondrial movement." Neurobiology of Disease 127 (July 2019): 410–18. http://dx.doi.org/10.1016/j.nbd.2019.03.021.

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24

Jang, Won Hee, and Dae-Hyun Seog. "PtdIns(3,5)P25-phosphatase Fig4 Interacts with Kinesin Superfamily 5A (KIF5A)." Journal of Life Science 24, no. 1 (January 30, 2014): 14–19. http://dx.doi.org/10.5352/jls.2014.24.1.14.

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25

Perić, Stojan, Vladana Marković, Ayşe Candayan, Els De Vriendt, Nikola Momčilović, Andrija Savić, Nataša Dragašević-Mišković, et al. "Phenotypic and Genetic Heterogeneity of Adult Patients with Hereditary Spastic Paraplegia from Serbia." Cells 11, no. 18 (September 8, 2022): 2804. http://dx.doi.org/10.3390/cells11182804.

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Hereditary spastic paraplegia (HSP) is among the most genetically diverse of all monogenic diseases. The aim was to analyze the genetic causes of HSP among adult Serbian patients. The study comprised 74 patients from 65 families clinically diagnosed with HSP during a nine-year prospective period. A panel of thirteen genes was analyzed: L1CAM (SPG1), PLP1 (SPG2), ATL1 (SPG3A), SPAST (SPG4), CYP7B1 (SPG5A), SPG7 (SPG7), KIF5A (SPG10), SPG11 (SPG11), ZYFVE26 (SPG15), REEP1 (SPG31), ATP13A2 (SPG78), DYNC1H1, and BICD2 using a next generation sequencing-based technique. A copy number variation (CNV) test for SPAST, SPG7, and SPG11 was also performed. Twenty-three patients from 19 families (29.2%) had conclusive genetic findings, including 75.0% of families with autosomal dominant and 25.0% with autosomal recessive inheritance, and 15.7% of sporadic cases. Twelve families had mutations in the SPAST gene, usually with a pure HSP phenotype. Three sporadic patients had conclusive findings in the SPG11 gene. Two unrelated patients carried a homozygous pathogenic mutation c.233T>A (p.L78*) in SPG7 that is a founder Roma mutation. One patient had a heterozygous de novo variant in the KIF5A gene, and one had a compound heterozygous mutation in the ZYFVE26 gene. The combined genetic yield of our gene panel and CNV analysis for HSP was around 30%. Our findings broaden the knowledge on the genetic epidemiology of HSP, with implications for molecular diagnostics in this region.

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Campbell, P. D., K. Shen, M. R. Sapio, T. D. Glenn, W. S. Talbot, and F. L. Marlow. "Unique Function of Kinesin Kif5A in Localization of Mitochondria in Axons." Journal of Neuroscience 34, no. 44 (October 29, 2014): 14717–32. http://dx.doi.org/10.1523/jneurosci.2770-14.2014.

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Ebbing, Bettina, Klaudiusz Mann, Agata Starosta, Johann Jaud, Ludger Schöls, Rebecca Schüle, and Günther Woehlke. "Effect of spastic paraplegia mutations in KIF5A kinesin on transport activity." Human Molecular Genetics 17, no. 9 (January 18, 2008): 1245–52. http://dx.doi.org/10.1093/hmg/ddn014.

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Nam, D. E., J. H. Woo, M. J. Kim, S. Y. Shin, B. O. Choi, and K. W. Chung. "Wide phenotypic spectrum of axonal peripheral neuropathy patients with KIF5A mutations." Journal of the Neurological Sciences 381 (October 2017): 380. http://dx.doi.org/10.1016/j.jns.2017.08.3288.

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29

Tsukasaki, Yoshikazu, Hirotoshi Kamata, Julia Wang, Tsuyoshi Sakai, Reiko Ikebe, Ann Jeffers, Boren Jake, et al. "KIF5A is Responsible for Collagen Transport of Myofibroblasts during Pleural Fibrosis." Biophysical Journal 112, no. 3 (February 2017): 238a. http://dx.doi.org/10.1016/j.bpj.2016.11.1304.

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Blair, Marcia A., Shaochun Ma, and Peter Hedera. "Mutation in KIF5A can also cause adult-onset hereditary spastic paraplegia." Neurogenetics 7, no. 1 (February 18, 2006): 47–50. http://dx.doi.org/10.1007/s10048-005-0027-8.

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31

Reid, Evan, Mark Kloos, Allison Ashley-Koch, Lori Hughes, Simon Bevan, Ingrid K. Svenson, Felicia Lennon Graham, et al. "A Kinesin Heavy Chain (KIF5A) Mutation in Hereditary Spastic Paraplegia (SPG10)." American Journal of Human Genetics 71, no. 5 (November 2002): 1189–94. http://dx.doi.org/10.1086/344210.

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32

Yoo, Ki-Seo, Kina Lee, and Hyong Kyu Kim. "Dendritic transport of postsynaptic density protein 95 (PSD-95) by KIF5A." IBRO Reports 6 (September 2019): S296—S297. http://dx.doi.org/10.1016/j.ibror.2019.07.917.

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33

Yokota, Satoshi, Sahil H. Shah, Emma Lee Huie, Runxia Rain Wen, Ziming Luo, and Jeffrey L. Goldberg. "Kif5a Regulates Mitochondrial Transport in Developing Retinal Ganglion Cells In Vitro." Investigative Opthalmology & Visual Science 64, no. 3 (March 2, 2023): 4. http://dx.doi.org/10.1167/iovs.64.3.4.

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34

Takemura, R., T. Nakata, Y. Okada, H. Yamazaki, Z. Zhang, and N. Hirokawa. "mRNA expression of KIF1A, KIF1B, KIF2, KIF3A, KIF3B, KIF4, KIF5, and cytoplasmic dynein during axonal regeneration." Journal of Neuroscience 16, no. 1 (January 1, 1996): 31–35. http://dx.doi.org/10.1523/jneurosci.16-01-00031.1996.

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35

Rydzanicz, M., M. Jagła, J. Kosinska, T. Tomasik, A. Sobczak, A. Pollak, I. Herman-Sucharska, A. Walczak, P. Kwinta, and R. Płoski. "KIF5A de novomutation associated with myoclonic seizures and neonatal onset progressive leukoencephalopathy." Clinical Genetics 91, no. 5 (September 16, 2016): 769–73. http://dx.doi.org/10.1111/cge.12831.

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36

Wang, Lina, and Anthony Brown. "A hereditary spastic paraplegia mutation in kinesin-1A/KIF5A disrupts neurofilament transport." Molecular Neurodegeneration 5, no. 1 (2010): 52. http://dx.doi.org/10.1186/1750-1326-5-52.

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37

Saez-Atienzar, Sara, Clifton L. Dalgard, Jinhui Ding, Adriano Chiò, Camile Alba, Dan N. Hupalo, Matthew D. Wilkerson, et al. "Identification of a pathogenic intronic KIF5A mutation in an ALS-FTD kindred." Neurology 95, no. 22 (October 19, 2020): 1015–18. http://dx.doi.org/10.1212/wnl.0000000000011064.

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38

Fichera, M., M. Lo Giudice, M. Falco, M. Sturnio, S. Amata, O. Calabrese, S. Bigoni, E. Calzolari, and M. Neri. "Evidence of kinesin heavy chain (KIF5A) involvement in pure hereditary spastic paraplegia." Neurology 63, no. 6 (September 27, 2004): 1108–10. http://dx.doi.org/10.1212/01.wnl.0000138731.60693.d2.

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39

Liu, Y. T., M. Laura, J. Hersheson, A. Horga, Z. Jaunmuktane, S. Brandner, A. Pittman, et al. "Extended phenotypic spectrum of KIF5A mutations: From spastic paraplegia to axonal neuropathy." Neurology 83, no. 7 (July 9, 2014): 612–19. http://dx.doi.org/10.1212/wnl.0000000000000691.

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40

Tessa, A., G. Silvestri, M. F. de Leva, A. Modoni, P. S. Denora, M. Masciullo, M. T. Dotti, et al. "A novel KIF5A/SPG10 mutation in spastic paraplegia associated with axonal neuropathy." Journal of Neurology 255, no. 7 (June 2, 2008): 1090–92. http://dx.doi.org/10.1007/s00415-008-0840-8.

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41

Kawasaki, Takashi, Kanta Kurauchi, Akira Higashihata, Tomonori Deguchi, Yuji Ishikawa, Masatake Yamauchi, Motoe Sasanuma, et al. "Transgenic medaka fish which mimic the endogenous expression of neuronal kinesin, KIF5A." Brain Research 1480 (October 2012): 12–21. http://dx.doi.org/10.1016/j.brainres.2012.08.047.

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42

Forsberg, Karin, Karin Graffmo, Bente Pakkenberg, Markus Weber, Martin Nielsen, Stefan Marklund, Thomas Brännström, and Peter Munch Andersen. "Misfolded SOD1 inclusions in patients with mutations in C9orf72 and other ALS/FTD-associated genes." Journal of Neurology, Neurosurgery & Psychiatry 90, no. 8 (April 16, 2019): 861–69. http://dx.doi.org/10.1136/jnnp-2018-319386.

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ObjectiveA hallmark of amyotrophic lateral sclerosis (ALS) caused by mutations in superoxide dismutase-1 (SOD1) are inclusions containing SOD1 in motor neurons. Here, we searched for SOD1-positive inclusions in 29 patients carrying ALS-linked mutations in six other genes.MethodsA panel of antibodies that specifically recognise misfolded SOD1 species were used for immunohistochemical investigations of autopsy tissue.ResultsThe 18 patients with hexanucleotide-repeat-expansions in C9orf72 had inclusions of misfolded wild type (WT) SOD1WT in spinal motor neurons. Similar inclusions were occasionally observed in medulla oblongata and in the motor cortex and frontal lobe. Patients with mutations in FUS, KIF5A, NEK1, ALSIN or VAPB, carried similar SOD1WT inclusions. Minute amounts of misSOD1WT inclusions were detected in 2 of 20 patients deceased from non-neurological causes and in 4 of 10 patients with other neurodegenerative diseases. Comparison was made with 17 patients with 9 different SOD1 mutations. Morphologically, the inclusions in patients with mutations in C9orf72HRE, FUS, KIF5A, NEK1, VAPB and ALSIN resembled inclusions in patients carrying the wildtype-like SOD1D90A mutation, whereas patients carrying unstable SOD1 mutations (A4V, V5M, D76Y, D83G, D101G, G114A, G127X, L144F) had larger skein-like SOD1-positive inclusions.Conclusions and relevanceAbundant inclusions containing misfolded SOD1WT are found in spinal and cortical motor neurons in patients carrying mutations in six ALS-causing genes other than SOD1. This suggests that misfolding of SOD1WT can be part of a common downstream event that may be pathogenic. The new anti-SOD1 therapeutics in development may have applications for a broader range of patients.

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43

Baron, Desiree M., Adam R. Fenton, Sara Saez-Atienzar, Anthony Giampetruzzi, Aparna Sreeram, Shankaracharya, Pamela J. Keagle, et al. "ALS-associated KIF5A mutations abolish autoinhibition resulting in a toxic gain of function." Cell Reports 39, no. 1 (April 2022): 110598. http://dx.doi.org/10.1016/j.celrep.2022.110598.

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44

de Fuenmayor-Fernández de la Hoz, Carlos Pablo, Aurelio Hernández-Laín, Montse Olivé, María Teresa Sánchez-Calvín, Juan Francisco Gonzalo-Martínez, and Cristina Domínguez-González. "Adult-onset distal spinal muscular atrophy: a new phenotype associated with KIF5A mutations." Brain 142, no. 12 (October 15, 2019): e66-e66. http://dx.doi.org/10.1093/brain/awz317.

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45

Faruq, Mohammed, Deepak Kumar, Saruchi Wadhwa, Uzma Shamim, Aradhana Mathur, Shaista Parveen, Ajay Garg, and Achal K. Srivastava. "Intrafamilial variable spastic paraplegia/ataxia/ALS phenotype linked to a novel KIF5A mutation." Clinical Genetics 96, no. 3 (July 8, 2019): 271–73. http://dx.doi.org/10.1111/cge.13585.

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46

Musumeci, Olimpia, Maria Teresa Bassi, Anna Mazzeo, Marina Grandis, Claudia Crimella, Andrea Martinuzzi, and Antonio Toscano. "A novel mutation in KIF5A gene causing hereditary spastic paraplegia with axonal neuropathy." Neurological Sciences 32, no. 4 (November 24, 2010): 665–68. http://dx.doi.org/10.1007/s10072-010-0445-8.

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47

Gu, XiaoJing, ChunYu Li, YongPing Chen, QianQian Wei, Bei Cao, RuWei Ou, XiaoQin Yuan, et al. "Mutation screening of the KIF5A gene in Chinese patients with amyotrophic lateral sclerosis." Journal of Neurology, Neurosurgery & Psychiatry 90, no. 2 (June 28, 2018): 245–46. http://dx.doi.org/10.1136/jnnp-2018-318395.

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48

Lorenzo, Damaris N., Alexandra Badea, Ruobo Zhou, Peter J. Mohler, Xiaowei Zhuang та Vann Bennett. "βII-spectrin promotes mouse brain connectivity through stabilizing axonal plasma membranes and enabling axonal organelle transport". Proceedings of the National Academy of Sciences 116, № 31 (17 червня 2019): 15686–95. http://dx.doi.org/10.1073/pnas.1820649116.

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βII-spectrin is the generally expressed member of the β-spectrin family of elongated polypeptides that form micrometer-scale networks associated with plasma membranes. We addressed in vivo functions of βII-spectrin in neurons by knockout of βII-spectrin in mouse neural progenitors. βII-spectrin deficiency caused severe defects in long-range axonal connectivity and axonal degeneration. βII-spectrin–null neurons exhibited reduced axon growth, loss of actin–spectrin-based periodic membrane skeleton, and impaired bidirectional axonal transport of synaptic cargo. We found that βII-spectrin associates with KIF3A, KIF5B, KIF1A, and dynactin, implicating spectrin in the coupling of motors and synaptic cargo. βII-spectrin required phosphoinositide lipid binding to promote axonal transport and restore axon growth. Knockout of ankyrin-B (AnkB), a βII-spectrin partner, primarily impaired retrograde organelle transport, while double knockout of βII-spectrin and AnkB nearly eliminated transport. Thus, βII-spectrin promotes both axon growth and axon stability through establishing the actin–spectrin-based membrane-associated periodic skeleton as well as enabling axonal transport of synaptic cargo.

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49

Brenner, David, Angela Rosenbohm, Rüstem Yilmaz, Kathrin Müller, Torsten Grehl, Susanne Petri, Thomas Meyer, et al. "Reply: Adult-onset distal spinal muscular atrophy: a new phenotype associated with KIF5A mutations." Brain 142, no. 12 (October 15, 2019): e67-e67. http://dx.doi.org/10.1093/brain/awz306.

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50

Rinaldi, Fabrizio, Maria T. Bassi, Alice Todeschini, Silvia Rota, Alessia Arnoldi, Alessandro Padovani, and Massimiliano Filosto. "A Novel Mutation in Motor Domain of KIF5A Associated With an HSP/Axonal Neuropathy Phenotype." Journal of Clinical Neuromuscular Disease 16, no. 3 (March 2015): 153–58. http://dx.doi.org/10.1097/cnd.0000000000000063.

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