Ask about this productRelated genes to: KIF5A Blocking Peptide
- Gene:
- KIF5A NIH gene
- Name:
- kinesin family member 5A
- Previous symbol:
- SPG10
- Synonyms:
- D12S1889, NKHC, MY050
- Chromosome:
- 12q13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-08-24
- Date modifiied:
- 2016-11-15
Related products to: KIF5A Blocking Peptide
Related articles to: KIF5A Blocking Peptide
- Spinocerebellar Ataxia type 2 (SCA2) and Amyotrophic Lateral Sclerosis type 13 (ALS13) are triggered by polyglutamine expansion in Ataxin-2 (ATXN2). To understand these neurodegenerative disorders at the molecular level, the brains of 10-month-old -CAG100-knockin mice were analyzed as microglial, astroglial and neuronal fractions via global RNA sequencing. Data were validated by comparison with the spinal cord oligonucleotide microarray profile or filtered by RNA-seq consistency. Here, we show that the mutation causes a massive inflammatory response in microglia and a reciprocal loss of neuronal transcripts in glial fractions, suggesting severe synapse loss. Beyond these general neurodegenerative signs, we identify pathognomonic changes in the machinery for protein translation and RNA splicing. Glial fractions showed upregulation of (to 2082%), , , , , , , , and as an unspecific neuroinflammatory signature, versus downregulation of axonal (to <19%), and synaptic , , , and mRNAs correlating with circuit disconnection. In all fractions, reductions in , , and were noted versus disease-specific inductions of ribosomal subunits, presumably mirroring the partial loss-of-function of ATXN2 as RNA translation modulator. Selective accumulations of embryonic factors and versus downregulation of adult specify the mutation impact on splicing and translation elongation. As a potential underpinning of toxic gain-of-function, the proteostasis transcript appeared increased in astroglial and microglial fractions. These transcriptome data suggest altered ribosomal and spliceosome machinery, with massive microgliosis versus mild astrogliosis, at the core of SCA2 and ALS13. - Source: PubMed
Publication date: 2026/04/15
Auburger GeorgKandi Arvind ReddyVutukuri RajkumarAlmaguer-Mederos Luis-EnriqueGispert SuzanaSen Nesli-EceKey Jana - To explore the mechanism by which alpha-lipoic acid (ALA) regulates mitochondrial axonal transport to protect the sciatic nerve in diabetic rats. - Source: PubMed
Publication date: 2026/04/01
Tian JiaxinAn JingwenSong LinchunZhang WangChen DieZhang TianyaBen Ying - Spinal muscular atrophy (SMA) is a devastating neuromuscular disorder caused by mutations in the survival motor neuron 1 (SMN1) gene leading to decreased SMN protein levels and motor neuron dysfunction. SMN-restoring therapies offer clinical benefit, but the downstream molecular consequences of SMN reduction remain incompletely understood. SMN deficiency resulted in downregulation of kinesin heavy chain isoform 5A (KIF5A) in human neurons and in a mouse model of SMA. SMN associated with KIF5A mRNA and contributed to its stability. Reduced SMN levels impaired axon regeneration, which was rescued by KIF5A overexpression. Because KIF5A has also been connected to ALS, these findings provide evidence of a molecular link between SMA and ALS pathophysiology, highlighting KIF5A as an SMN-regulated factor. Our findings suggest that SMN-independent interventions targeting KIF5A could represent a complementary therapeutic approach for SMA and other motor neuron diseases. - Source: PubMed
Publication date: 2026/03/26
Akiyama TetsuyaZeng YiGuo CaiweiGautier OliviaKoepke LaurenLyons HeankelMolotsky ElanaBombosch Juliane SSianto OdiliaRoss Jay PHoang PhuongZhao LukeSpencer ColeSumner Charlotte JMonje MichelleDay John WGitler Aaron D - Mitochondrial trafficking ensures proper distribution of mitochondria in energy-demanding neural stem cells (NSCs) and neurons, by supplying ATP for neuronal function and survival. We studied the effects of xenoestrogen bisphenol-A (BPA), found in consumable plastic products, on axonal bi-directional mitochondrial trafficking/movement in neurons. Time-lapse live-cell imaging revealed that BPA exposure impaired anterograde and retrograde axonal mitochondrial trafficking, resulting in altered mitochondrial distribution and density in hippocampal NSCs-derived neurons. In silico docking studies identified plausible binding of BPA with Kinesin-1, Dynein, and Syntaphilin (SNPH). BPA postnatal exposure reduced mRNA expression and protein levels of mitochondrial trafficking motor proteins Kinesin-1(KIF5A) and Dynein, and increased mitochondrial static anchor protein SNPH in the rat hippocampus. BPA significantly reduced co-localization of KIF5A and Dynein with TOMM20, Nestin & β-III tubulin in vitro and Sox-2 & NeuN in vivo, and increased SNPH co-localization with TOMM20, Nestin & Sox-2, indicating impaired mitochondrial trafficking during NSCs proliferation and differentiation. Transmission Electron Microscopy revealed reduced axonal mitochondrial density, synaptic density, increased damaged mitochondria, and synaptic loss following BPA exposure. Pharmacological inhibition (Monastrol) and activation (Kinesore) of KIF5A mediated mitochondrial transport caused aggravated and mitigated BPA-mediated impairments in NSCs proliferation and neuronal differentiation. BPA-mediated inhibition of mitochondrial distribution, bioenergetics, and synaptic function was reversed by Kinesore, by increasing mitochondrial & synaptic density, mitochondrial movement, and reducing damaged synapses & mitochondria, leading to cognitive improvements. These findings implicate the role of Kinesin-1(KIF5A) in reversing BPA-mediated impaired mitochondrial transport, reduced hippocampal neurogenesis, and cognitive deficits in rats. - Source: PubMed
Publication date: 2026/03/14
Phoolmala Tiwari SaurabhYadav Ranjeet KumarChauhan Shweta SinghChaturvedi Rajnish Kumar - Recent studies have identified variants in the kinesin family member 5A () gene that predispose to amyotrophic lateral sclerosis (ALS). These ALS-linked variants lead to the exclusion of exon 27, resulting in the production of a mutated protein with an altered C-terminal region (KIF5A ΔExon27). Through whole genome sequencing, we identified a novel intronic variant, rs1057522322 (c.2993-6C > A; chr12:57582596C > A, GRCh38.p14), in a family segregating ALS. Our goal is to investigate the effect of this variant on exon 27 splicing and to assess its functional consequences on KIF5A-mediated cargo transport. - Source: PubMed
Publication date: 2026/03/11
Rouleau Guy AYu ZiqiRoss Jay PRochefort DanielLi BotingBornais KateChum MarvinFarhan Sali M KDion Patrick A