ePoster

DENDRITIC INTERACTIONS DURING INDUCTION OF PLASTICITY IN MOUSE HIPPOCAMPAL CA1 NEURONS <EM>EX VIVO</EM>

Xuelin Wang

University of Cambridge

FENS Forum 2026 (2026)
Barcelona, Spain
Board PS03-08AM-525

Presentation

Date TBA

Board: PS03-08AM-525

Poster preview

DENDRITIC INTERACTIONS DURING INDUCTION OF PLASTICITY IN MOUSE HIPPOCAMPAL CA1 NEURONS <EM>EX VIVO</EM> poster preview

Event Information

Poster Board

PS03-08AM-525

Abstract

Spike timing–dependent plasticity (STDP) is a physiological form of Hebbian learning in which the direction and magnitude of synaptic change depend on the precise timing of presynaptic and postsynaptic spikes. STDP is proposed to underlie learning, memory formation, and circuit refinement during development. STDP operates as a multi-factor plasticity rule, where both the sign and magnitude of plasticity are also influenced by additional synaptic, cellular, and neuromodulatory factors. One fundamental question regarding the quantitative rules governing STDP induction is whether the plasticity induced by one synaptic input affects the ability of subsequent inputs to induce STDP within the same neuron, depending on the timing of these inputs relative to the postsynaptic spike.

Using whole-cell patch-clamp recordings from hippocampal slices, I applied a novel stimulation paradigm (pre1–post–pre2) to probe interactions between converging excitatory inputs with distinct arrival times. Strikingly, an excitatory event preceding a post-before-pre pairing converted t-LTD into t-LTP, revealing sensitivity of STDP polarity to input sequence rather than spike timing alone. To investigate the underlying mechanisms, I examined the role of NMDA receptors (NMDARs) using pharmacological manipulations targeting the glutamate binding site, channel pore, and glycine co-agonist site. These experiments uncovered an unconventional form of t-LTD that depends on the glycine binding site and channel pore, but not the glutamate binding site, of presynaptic NMDARs. This profile is consistent with the involvement of GluN1/3-containing NMDARs, suggesting a glycine-activated, glutamate-independent mechanism for t-LTD during early development.

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