anti-Kinesin Family Member 5A (KIF5A) Antibodies

Zebrafish Kinesin Family Member 5A (KIF5A) interaction partners

1. Deletion of a kinesin I motor unmasks a mechanism of homeostatic axon-branching control by neurotrophin-3.

2. Our results shed light on Kinesin complexity and reveal determinants of specific Kif5A functions in mitochondrial transport, adaptor binding, and axonal maintenance.

Human Kinesin Family Member 5A (KIF5A) interaction partners

1. KIF5A p.Ala361Val cause spastic paraplegia and primary progressive multiple sclerosis.

2. ALS-associated mutations in KIF5A, are located at the C-terminal cargo-binding tail domain and patients harboring loss-of-function mutations displayed an extended survival relative to typical ALS cases.

3. This study found that the 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.

4. These results support our hypothesis that KIF5A is responsible for collagen transportation and secretion from HPMCs.

5. This study identified three pathogenic KIF5A mutations in Korean Charcot-Marie-Tooth neuropathy type 2 patients by whole exome sequencing. Two mutations (p.Arg204Trp and p.Arg280His) were previously reported, but p.Leu558Pro was determined to be a novel de novo mutation.

6. We conclude that reduced expression of axonal motor KIF5A may have important implications in determining axonal transport deficits and ongoing neurodegeneration in multiple sclerosis

7. Kinesin family member 5A protein (Kif5A) with hereditary spastic paraplegia (HSP)-causing mutations showed a variety of significantly reduced catalytic and mechanical activities as a result of each mutation, with the shared phenotype from each that motility was significantly reduced.

8. Variants in SPAST and KIF5A were the most common causes of autosomal dominant hereditary spastic paraplegia in Greece. The first nonsense mutation in KIF5A was identified in HSP patient.

9. De novo stop-loss frameshift variants in KIF5A result in a novel phenotype that includes severe infantile onset myoclonus, hypotonia, optic nerve abnormalities, dysphagia, apnea, and early developmental arrest.

10. KIF5A p.Ser974fs de novo mutation associated with myoclonic seizures and neonatal onset progressive leukoencephalopathy.

11. Zinc ion-mediated inhibition of KIF5A activity might be one molecular cause contributing to impaired transport processes within brain and other organs in cases of zinc dyshomeostasis.

12. This report describes the first known Asian family with a KIF5A mutation and broadens the clinical and electrophysiological spectrum associated with KIF5A-SPG10 mutations.

13. study describes 2 Spanish families with an adult onset complicated autosomal dominant hereditary spastic paraplegia with a mild sensory neuropathy; identified 2 novel mutations c.773 C>T and c.833 C>T in the KIF5A gene resulting in the P258L and P278L substitutions; both were located in the highly conserved kinesin motor domain of the protein

14. Kinesin-14 blocks microtubule nucleation in yeast and reveal that this inhibition is countered by the kinesin-5 protein, Cut7.[Cut7, Pkl1]

15. the novel mutation p.Leu259Gln in two siblings affected by Hereditary spastic paraplegia (HSP) complicated by deafness and in their father with a pure form of HSP.

16. Combining next-generation sequencing and conventional sequencing, study confirms that KIF5A mutations can cause variable phenotypes ranging from hereditary spastic paraplegia to Charcot-Marie-Tooth disease type 2

17. Conformations of microtubule-bound human kinesin-5 motor domain were visualised at successive steps in its ATPase cycle.

18. A review of the mechanism of pathogenesis involved in spastic paraplegia type 10 when KIF5A is inactivated by mutations.

19. Data suggest that the impairment of the microtubule-kinesin function by alpha-synuclein oligomers drives early neurite pathology.

20. This study extends the phenotype of SPG10 and argues for abnormalities in the axonal vesicular transport.

Mouse (Murine) Kinesin Family Member 5A (KIF5A) interaction partners

1. The authors concluded that kinesin-1 proteins KIF5A, -5B, and -5C are important in the anterograde transport of the majority of herpes simplex virus enveloped virions in neuronal axons and kinesin-3 proteins are less important.

2. These results support our hypothesis that KIF5A is responsible for collagen transportation and secretion from HPMCs.

3. Klf5 contributes to adult mouse corneal epithelial homeostasis by promoting (1) permeability barrier function through upregulation of Tjp1, Gkn1, Dsg1a, Lama3, and Lamb1, and (2) basal cell proliferation through upregulation of cyclin-D1 and suppression of phospho(Ser-10) p27/Kip1

4. Results from the present study reveal a new system mediated by kinesin-1 sorting in axons that differentially controls stability of arbor terminals.

5. Data suggest that KIF5 regulates gephyrin sorting by a mechanism that involves GSK3 activity.

6. KIF5-SNPH interaction mediates activity-induced immobilization of axonal mitochondria.

7. Found a role of KIF5A in process outgrowth and axonal transport of mitochondria, affecting motor neurons more severely than sensory neurons.

8. Expression of Kif5a in the mouse prefrontal cortex is modulated by a sequence variant (B2 SINE indel) in the 3' UTR of Comt (catechol-O-methyltransferase).

9. Data suggest that kinesin-1A is the principal anterograde motor for neurofilaments, that there may be functional redundancy among isoforms in neurofilament transport, and that anterograde and retrograde neurofilament motors are tightly coordinated.

10. assessement of the kinetics of the dystrobrevin-Kif5A interaction suggesting that the tertiary structure of dystrobrevin may play a role in regulating its interaction with Kif5a