Research Project
Grant-in-Aid for Challenging Exploratory Research
Synapse formation in the brain is partly mediated by a small subset of trans-synaptic cell adhesion molecules called synapse organizers. We found that PTPδ one of presynaptic synapse organizers, existed in multiple splice variants generated by insertions of 3, 6 and 4 amino-acid residue peptides (termed mini-exon peptides) in the extracellular immunoglobulin (Ig)-like domains. At least 8 splice variants in the Ig-like domains of PTPδ were expressed in the developing mouse brains. Proportions of these splice variants varied across brain regions and developmental stages. Furthermore, structural analyses of synapse-organizing complex of PTPδ and its ligands revealed the role of mini-exon peptides on the ligand recognition and synaptic differentiation. These results suggest that the choice of mini-exons may be determinants for selective pairing between PTPδ variants and their corresponding postsynaptic ligands to ensure the target specific synapse formation in the brain.
All 2015 2014 Other
All Journal Article (6 results) (of which Peer Reviewed: 5 results, Open Access: 5 results, Acknowledgement Compliant: 2 results) Presentation (17 results) (of which Int'l Joint Research: 1 results, Invited: 3 results) Book (2 results) Remarks (1 results)
Scientific Reports
Volume: 5 Pages: 9686
doi: 10.1038/srep09686.
Nature Communications
Volume: 6 Pages: 6926
doi: 10.1038/ncomms7926.
Amino Acids
Volume: 47 Pages: 79-86
doi: 10.1007/s00726-014-1847-3.
日本薬理学雑誌
Volume: 145 Pages: 187-192
Volume: 4 Pages: 6613
doi: 10.1038/srep06613.
Journal of Molecular and Cellular Cardiology
Volume: 72 Pages: 273-280
doi: 10.1016/j.yjmcc.2014.03.019.
http://www.med.u-toyama.ac.jp/molneurosci/index.html
