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Title 

Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn

 

PTPRT에 의한 신경시냅스 형성 조절

Authors 

So Hee LimS K KwonMyung Kyu LeeJeong Hee MoonDae Gwin JeongEun Ha ParkSeung Jun KimByoung Chul ParkSang Chul LeeS E RyuDae Yeul YuBong Hyun ChungE KimP K MyungJae-Ran Lee

Publisher 

Nature Publishing Group

Issue Date 

2009

Citation 

EMBO Journal, vol. 28, no. 22, pp. 3564-3578

Keywords 

Cell adhesion moleculeFynPTPRTSynapse formationTyrosine phosphorylation

Abstract 

The receptor-type protein tyrosine phosphatases (RPTPs) have been linked to signal transduction, cell adhesion, and neurite extension. PTPRT/RPTP is exclusively expressed in the central nervous system and regulates synapse formation by interacting with cell adhesion molecules and Fyn protein tyrosine kinase. Overexpression of PTPRT in cultured neurons increased the number of excitatory and inhibitory synapses by recruiting neuroligins that interact with PTPRT through their ecto-domains. In contrast, knockdown of PTPRT inhibited synapse formation and withered dendrites. Incubation of cultured neurons with recombinant proteins containing the extracellular region of PTPRT reduced the number of synapses by inhibiting the interaction between ecto-domains. Synapse formation by PTPRT was inhibited by phosphorylation of tyrosine 912 within the membrane-proximal catalytic domain of PTPRT by Fyn. This tyrosine phosphorylation reduced phosphatase activity of PTPRT and reinforced homophilic interactions of PTPRT, thereby preventing the heterophilic interaction between PTPRT and neuroligins. These results suggest that brain-specific PTPRT regulates synapse formation through interaction with cell adhesion molecules, and this function and the phosphatase activity are attenuated through tyrosine phosphorylation by the synaptic tyrosine kinase Fyn.

ISSN 

0261-4189

Link 

http://dx.doi.org/10.1038/emboj.2009.289

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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