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Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
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SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development.
Yeonsoo Choi1, Jungyong Nam1, Daniel J Whitcomb2
1Department of Biological Sciences, Korea Advanced Institute for Science and Technology (KAIST), Daejeon 305-701, Korea.
Scientific Reports
|May 27, 2016
Summary
Synapse formation involves adhesion molecules like SALM5, which interacts with LAR family phosphatases. This interaction is crucial for presynaptic differentiation and regulating synaptic strength in the brain.
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- Synaptogenic adhesion molecules are vital for synapse formation.
- SALM5/Lrfn5, linked to autism spectrum disorders and schizophrenia, induces presynaptic differentiation but its ligand is unknown.
Purpose of the Study:
- To identify the presynaptic ligand of SALM5.
- To elucidate the role of SALM5-ligand interactions in synapse development and function.
Main Methods:
- Co-immunoprecipitation assays to identify SALM5-interacting proteins.
- In vitro and in vivo assays to assess the functional impact of SALM5-LAR-RPTP interactions on presynaptic differentiation and synaptic transmission.
Main Results:
- SALM5 interacts with the Ig domains of LAR family receptor protein tyrosine phosphatases (LAR-RPTPs).
- These interactions are modulated by splice insert B in LAR-RPTPs and mediate SALM5-dependent presynaptic differentiation.
- SALM5 regulates AMPA receptor-mediated synaptic transmission via trans-synaptic interaction with presynaptic LAR-RPTPs.
Conclusions:
- Postsynaptic SALM5 promotes synapse development through trans-synaptic interaction with presynaptic LAR-RPTPs.
- SALM5-LAR-RPTP interactions are critical for regulating excitatory synaptic strength and may be relevant to neurological disorders.
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