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762 results on '"Matsumoto, Kunihiro"'

2. A cytidine deaminase regulates axon regeneration by modulating the functions of the Caenorhabditis elegans HGF/plasminogen family protein SVH-1.

Author

Shimizu, Tatsuhiro, Nomachi, Takafumi, Matsumoto, Kunihiro, and Hisamoto, Naoki

Subjects
CYTIDINE deaminase, HEMATOPOIETIC growth factors, CAENORHABDITIS elegans, NERVOUS system regeneration, AXONS, PLASMINOGEN
Abstract

The pathway for axon regeneration in Caenorhabditis elegans is activated by SVH-1, a growth factor belonging to the HGF/plasminogen family. SVH-1 is a dual-function factor that acts as an HGF-like growth factor to promote axon regeneration and as a protease to regulate early development. It is important to understand how SVH-1 is converted from a protease to a growth factor for axon regeneration. In this study, we demonstrate that cytidine deaminase (CDD) SVH-17/CDD-2 plays a role in the functional conversion of SVH-1. We find that the codon exchange of His-755 to Tyr in the Asp–His–Ser catalytic triad of SVH-1 can suppress the cdd-2 defect in axon regeneration. Furthermore, the stem hairpin structure around the His-755 site in svh-1 mRNA is required for the activation of axon regeneration by SVH-1. These results suggest that CDD-2 promotes axon regeneration by transforming the function of SVH-1 from a protease to a growth factor through modification of svh-1 mRNA. Author summary: The axon regeneration pathway in C. elegans is activated by SVH-1, a growth factor that belongs to the HGF/plasminogen family. SVH-1 is a dual-functional factor that promotes axon regeneration as an HGF-like growth factor and regulates development as a plasminogen-like protease. It is crucial to understand the mechanism by which SVH-1 transforms from a protease to a growth factor during axon regeneration. In this study, we demonstrate that CDD-2, a cytidine deaminase, is critical for converting SVH-1 function from a protease to a growth factor by modifying svh-1 mRNA. [ABSTRACT FROM AUTHOR]

Published
2024
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48. Identification of Guanylyl Cyclases that function in thermosensory neurons of Caenorhabditis elegans

Author

Inada, Hitoshi, Ito, Hiroko, Satterlee, John, Sengupta, Piali, Matsumoto, Kunihiro, and Mori, Ikue

Subjects
Neurons -- Research, Caenorhabditis elegans -- Research, Caenorhabditis elegans -- Genetic aspects, Guanylate cyclase -- Research, Guanylate cyclase -- Genetic aspects, Guanylate cyclase -- Identification and classification, Biological sciences
Abstract

The nematode Caenorhabditis elegans senses temperature primarily via the AFD thermosensory neurons in the head. The response to temperature can be observed as a behavior called thermotaxis on thermal gradients. It has been shown that a cyclic nucleotide-gated ion channel (CNG channel) plays a critical role in thermosensation in AFD. To further identify the thermosensory mechanisms in AFD, we attempted to identity components that function upstream of the CNG channel by a reverse genetic approach. Genetic and behavioral analyses showed that three members of a subfamily of gcy genes (gcy-8, gcy,-18, and gcy-23) encoding guanylyl cyclases were essential for thermotaxis in C. elegans. Promoters of each gene drove reporter gene expression exclusively in the AFD neurons and, moreover tagged proteins were localized to the Sensory endings of AFD. Single mutants of each gcy gene showed almost normal thermotaxis. However animals canting double and triple mutations in these genes showed defective thermotaxis behavior. The abnormal phenotype of the gcy triple mutants was rescued by expression of any one of the three GCY proteins in the AFD neurons. These results suggest that three guanylyl cyclases function redundantly in the AFD neurons to mediate thermosensation by C. elegans.

Published
2006

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