SynActive-PSD95-FLAG, a genetically encoded probe consisting of FLAG-tagged PSD- 95 endowed with activity-dependent local translation and expression enrichment at potentiating dendritic spines, provides new insight into the molecular substrates of hippocampal learning and a novel tool to study the proteome of potentiated synapses.
The cross-validation with patient transcriptomic data, demonstrated that the epileptic synapse undergoes a pathological shift and the upregulation of the auxiliary proteins functionally overpowers the established LTD machinery and prevents LTD consolidation.
Pacheriyil Meghna, S. Kateriya, Pradeep Punnakkal· bioRxiv· 0 citations
Silent synapses represent a unique class of synaptic connections that are non-functional at rest but possess the potential to become functional, serving as a critical reservoir for neural plasticity. Their activation mechanisms not only challenge traditional models of synaptic maturation but also provide novel insights...
Yong-Li Li, Yong Liao, Shou-Yao Zhang et al.· Frontiers in Synaptic Neuros...· 0 citations
Findings identify PKCα as part of a signaling program associated with synaptic function and support a role for PKCα-dependent processes in adaptive updating of learned fear in Prkca-/- mice.
Lulu An, Miyoung Yang, Q. Ding et al.· Neurobiology of Stress· 0 citations
Long-term memory is widely thought to depend on activity-dependent synaptic plasticity and the structural remodeling that accompanies it, yet direct causal evidence that this remodeling is required for memory storage has been lacking. A case in point is the formation of dendritic spines: new spines appear following lea...
Hiranmay Joag, Patricio Opazo, Kenta M. Hagihara et al.· bioRxiv· 0 citations
Learning requires dynamic changes in synaptic protein composition. Most synaptic proteomic studies capture endpoint snapshots following training, overlooking molecular changes occurring during learning itself. We previously established TurboID proximity proteomics as an approach to capture protein-level changes during...
Aelon Rahmani, Michaela E. Johnson, Rosemary A. Coleman et al.· bioRxiv· 0 citations
The cellular form of the prion protein (PrPC) is known for its involvement in the pathogenesis of prion diseases. Recent research implicates the physiological isoform of PrP in neuronal development, excitability, and synaptic plasticity, as well as in other biological processes. However, its precise function in the dev...
Anna Burato, Alessio Di Clemente, Camilla Lodetti et al.· bioRxiv· 1 citation
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