Abstract:
:Presynaptic neurexins (Nrxs) and type IIa receptor-type protein tyrosine phosphatases (RPTPs) organize synapses through a network of postsynaptic ligands. We show that leucine-rich-repeat transmembrane neuronal proteins (LRRTMs) differentially engage the protein domains of Nrx but require its heparan sulfate (HS) modification to induce presynaptic differentiation. Binding to the HS of Nrx is sufficient for LRRTM3 and LRRTM4 to induce synaptogenesis. We identify mammalian Nrx1γ as a potent synapse organizer and reveal LRRTM4 as its postsynaptic ligand. Mice expressing a mutant form of LRRTM4 that cannot bind to HS show structural and functional deficits at dentate gyrus excitatory synapses. Through the HS of Nrx, LRRTMs also recruit PTPσ to induce presynaptic differentiation but function to varying degrees in its absence. PTPσ forms a robust complex with Nrx, revealing an unexpected interaction between the two presynaptic hubs. These findings underscore the complex interplay of synapse organizers in specifying the molecular logic of a neural circuit.
journal_name
Neuronjournal_title
Neuronauthors
Roppongi RT,Dhume SH,Padmanabhan N,Silwal P,Zahra N,Karimi B,Bomkamp C,Patil CS,Champagne-Jorgensen K,Twilley RE,Zhang P,Jackson MF,Siddiqui TJdoi
10.1016/j.neuron.2020.01.003subject
Has Abstractpub_date
2020-04-08 00:00:00pages
108-125.e12issue
1eissn
0896-6273issn
1097-4199pii
S0896-6273(20)30003-9journal_volume
106pub_type
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