PUBLICATION
Extracellular Pgk1 interacts neural membrane protein enolase-2 to improve the neurite outgrowth of motor neurons
- Authors
- Fu, C.Y., Chen, H.Y., Lin, C.Y., Chen, S.J., Sheu, J.C., Tsai, H.J.
- ID
- ZDB-PUB-250321-7
- Date
- 2023
- Source
- Communications biology 6: 849849 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
- none
- PubMed
- 37582937 Full text @ Commun Biol
Citation
Fu, C.Y., Chen, H.Y., Lin, C.Y., Chen, S.J., Sheu, J.C., Tsai, H.J. (2023) Extracellular Pgk1 interacts neural membrane protein enolase-2 to improve the neurite outgrowth of motor neurons. Communications biology. 6:849849.
Abstract
Understanding the molecular interaction between ligand and receptor is important for providing the basis for the development of regenerative drugs. Although it has been reported that extracellular phosphoglycerate kinase 1 (Pgk1) can promote the neurite outgrowth of motoneurons, the Pgk1-interacting neural receptor remains unknown. Here we show that neural membranous Enolase-2 exhibits strong affinity with recombinant Pgk1-Flag, which is also evidently demonstrated by immunoelectron microscopy. The 325th-417th domain of Pgk1 interacts with the 405th-431st domain of Enolase-2, but neither Enolase-1 nor Enolase-3, promoting neurite outgrowth. Combining Pgk1 incubation and Enolase-2 overexpression, we demonstrate a highly significant enhancement of neurite outgrowth of motoneurons through a reduced p-P38-T180/p-Limk1-S323/p-Cofilin signaling. Collectively, extracellular Pgk1 interacts neural membrane receptor Enolase-2 to reduce the P38/Limk1/Cofilin signaling which results in promoting neurite outgrowth. The extracellular Pgk1-specific neural receptor found in this study should provide a material for screening potential small molecule drugs that promote motor nerve regeneration.
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