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Kif2a operates as a gatekeeper of nociception in sensory neurons [RNA-seq - 3 months]

ABSTRACT: Kif2a operates as a gatekeeper of nociception in sensory neurons [RNA-seq - 3 months]

PROVIDER: PRJNA924037 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR23085474.fastq.gz	Fastqsanger.gz
	SRR23085475.fastq.gz	Fastqsanger.gz
	SRR23085476.fastq.gz	Fastqsanger.gz
	SRR23085477.fastq.gz	Fastqsanger.gz
	SRR23085478.fastq.gz	Fastqsanger.gz

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Kif2a operates as a gatekeeper of nociception in sensory neurons [RNA-seq - 6 months]

Project description:Kif2a operates as a gatekeeper of nociception in sensory neurons [RNA-seq - 6 months]

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Kif2a operates as a gatekeeper of nociception in sensory neurons [RNA-seq - 6 months]

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Project description:Kif2a operates as a gatekeeper of nociception in sensory neurons [RNA-seq - 1 month]

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Kif2a operates as a gatekeeper of nociception in sensory neurons [RNA-seq - 1 month]

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Kif2a operates as a gatekeeper of nociception in sensory neurons

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KIF2A stabilises intercellular bridge microtubules to maintain mouse embryonic stem cell cytokinesis

Project description:Cytokinesis, the final stage of cell division, serves to physically separate daughter cells. In cultured naïve mouse embryonic stem cells cytokinesis lasts unusually long. Here, we describe a novel function for the kinesin-13 member KIF2A in this process. In genome-engineered mouse embryonic stem cells we find that KIF2A localises to spindle poles during metaphase and regulates spindle length in a manner consistent with its known role as microtubule minus-end depolymerase. By contrast, during cytokinesis we observe tight binding of KIF2A to intercellular bridge microtubules. At this stage KIF2A maintains microtubule length and number, and controls microtubule acetylation. We propose that the conversion of KIF2A from a depolymerase to a stabiliser is driven both by the inhibition of its ATPase activity, which increases lattice affinity, and a preference for compacted lattices. In turn, KIF2A might maintain the compacted microtubule state at the intercellular bridge, thereby dampening acetylation. As KIF2A depletion causes pluripotency problems and affects mRNA homeostasis our results furthermore indicate that KIF2A-mediated microtubule stabilisation prolongs cytokinesis to maintain pluripotency.

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Wnt signaling recruits KIF2A to the spindle to ensure chromosome congression during mitosis

Project description:Canonical Wnt signaling plays critical roles in development and tissue renewal by regulating β-catenin target genes. Recent evidence showed that β-catenin-independent Wnt signaling is also required for faithful execution of mitosis. This mitotic Wnt signaling functions through Wnt-dependent stabilization of proteins (Wnt/STOP), as well as through components of the LRP6 signalosome. However, the targets and specific functions of mitotic Wnt signaling still remain uncharacterized. Using phosphoproteomics, we identified that Wnt signaling regulates the microtubule depolymerase KIF2A during mitosis. We found that Dishevelled recruits KIF2A via its N-terminal and motor domains, which is further promoted upon LRP6 signalosome formation during mitosis. We show that Wnt signaling modulates KIF2A interaction with PLK1, which is critical for KIF2A localization and the assembly of a bipolar mitotic spindle. Accordingly, Wnt signaling promotes chromosome congression during metaphase by monitoring KIF2A protein levels at the spindle poles both in somatic cells and in pluripotent stem cells. Our findings highlight a novel function of Wnt signaling during cell division, which could have important implications for genome maintenance, notably in stem cells.

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Project description:Rac1, a member of the small G protein Rho family, has been implicated in neurodegenerative diseases. However, its role in axon degeneration is not fully understood. Here we found that activation of Rac1 exacerbated axonal transport damage in an experimental glaucoma model. Inhibiting Rac1 activity by genetic or pharmacological methods alleviated the dysfunction of axonal transport and improved the integrity of microtubule by upregulating the expression of β-III tubulin and myelin basic protein. Rac1 interacted with Sirt1, a key molecule of Wallerian degeneration, which regulated the activity of PAK1, a downstream molecule of Rac1. Furthermore, Rac1 modulated Kif motors at the transcriptional level, among which Kif2a, a lysosome-location regulator, was negatively regulated by Rac1. Intravitreal injection of Kif2a siRNA reversed the improvement of Rac1 inhibition-mediated axonal transport through reducing autophagolysosomes. Our results suggest that Rac1/Kif2a accelerates the process of RGC axon degeneration by impairing the autophagic flux in glaucoma, which may be an intriguing therapy target for glaucoma.

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