Sell_2024_bioRxiv__

Reference

Title : Glutamate signaling and neuroligin\/neurexin adhesion play opposing roles that are mediated by major histocompatibility complex I molecules in cortical synapse formation - Sell_2024_bioRxiv__
Author(s) : Sell GL , Barrow SL , McAllister AK
Ref : bioRxiv , : , 2024
Abstract :

Although neurons release neurotransmitter before contact, the role for this release in synapse formation remains unclear. Cortical synapses do not require synaptic vesicle release for formation (1-4) , yet glutamate clearly regulates glutamate receptor trafficking (5,6) and induces spine formation (7-11) . Using a culture system to dissect molecular mechanisms, we found that glutamate rapidly decreases synapse density specifically in young cortical neurons in a local and calcium-dependent manner through decreasing NMDAR transport and surface expression as well as co-transport with neuroligin (NL1). Adhesion between NL1 and neurexin 1 protects against this glutamate-induced synapse loss. Major histocompatibility I (MHCI) molecules are required for the effects of glutamate in causing synapse loss through negatively regulating NL1 levels. Thus, like acetylcholine at the NMJ, glutamate acts as a dispersal signal for NMDARs and causes rapid synapse loss unless opposed by NL1-mediated trans-synaptic adhesion. Together, glutamate, MHCI and NL1 mediate a novel form of homeostatic plasticity in young neurons that induces rapid changes in NMDARs to regulate when and where nascent glutamatergic synapses are formed.

PubMedSearch : Sell_2024_bioRxiv__
PubMedID: 38496590

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Citations formats

Sell GL, Barrow SL, McAllister AK (2024)
Glutamate signaling and neuroligin\/neurexin adhesion play opposing roles that are mediated by major histocompatibility complex I molecules in cortical synapse formation
bioRxiv :

Sell GL, Barrow SL, McAllister AK (2024)
bioRxiv :