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Postsynaptic TrkC and presynaptic PTPs function as a bidirectional excitatory synaptic organizing complex.

Authors: Takahashi, Hideto  Arstikaitis, Pamela  Prasad, Tuhina  Bartlett, Thomas E  Wang, Yu Tian  Murphy, Timothy H  Craig, Ann Marie 
Citation: Takahashi H, etal., Neuron. 2011 Jan 27;69(2):287-303. doi: 10.1016/j.neuron.2010.12.024.
Pubmed: (View Article at PubMed) PMID:21262467
DOI: Full-text: DOI:10.1016/j.neuron.2010.12.024

Neurotrophin receptor tyrosine kinases (Trks) have well-defined trophic roles in nervous system development through kinase activation by neurotrophins. Yet Trks have typical cell-adhesion domains and express noncatalytic isoforms, suggesting additional functions. Here we discovered noncatalytic TrkC in an unbiased hippocampal neuron-fibroblast coculture screen for proteins that trigger differentiation of neurotransmitter release sites in axons. All TrkC isoforms, but not TrkA or TrkB, function directly in excitatory glutamatergic synaptic adhesion by neurotrophin-independent high-affinity trans binding to axonal protein tyrosine phosphatase receptor PTPs. PTPs triggers and TrkC mediates clustering of postsynaptic molecules in dendrites, indicating bidirectional synaptic organizing functions. Effects of a TrkC-neutralizing antibody that blocks TrkC-PTPs interaction and TrkC knockdown in culture and in vivo reveal essential roles of TrkC-PTPs in glutamatergic synapse formation. Thus, postsynaptic TrkC trans interaction with presynaptic PTPs generates bidirectional adhesion and recruitment essential for excitatory synapse development and positions these signaling molecules at the center of synaptic pathways.

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RGD Object Information
RGD ID: 13702219
Created: 2018-07-18
Species: All species
Last Modified: 2018-07-18
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.