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- W2884299905 abstract "The protein kinase C (PKC) enzymes have long been established as critical for synaptic plasticity. However, it is unknown whether Ca2+-dependent PKC isozymes are activated in dendritic spines during plasticity and, if so, how this synaptic activity is encoded by PKC. Here, using newly developed, isozyme-specific sensors, we demonstrate that classical isozymes are activated to varying degrees and with distinct kinetics. PKCα is activated robustly and rapidly in stimulated spines and is the only isozyme required for structural plasticity. This specificity depends on a PDZ-binding motif present only in PKCα. The activation of PKCα during plasticity requires both NMDA receptor Ca2+ flux and autocrine brain-derived neurotrophic factor (BDNF)–TrkB signaling, two pathways that differ vastly in their spatiotemporal scales of signaling. Our results suggest that, by integrating these signals, PKCα combines a measure of recent, nearby synaptic plasticity with local synaptic input, enabling complex cellular computations such as heterosynaptic facilitation of plasticity necessary for efficient hippocampus-dependent learning. Through the development of novel PKC biosensors, the authors describe how PKCα, but not other classical isozymes, facilitates plasticity in dendritic regions through the integration of recent synaptic plasticity with current, local synaptic input." @default.
- W2884299905 created "2018-08-03" @default.
- W2884299905 creator A5003467670 @default.
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- W2884299905 date "2018-07-16" @default.
- W2884299905 modified "2023-10-10" @default.
- W2884299905 title "PKCα integrates spatiotemporally distinct Ca2+ and autocrine BDNF signaling to facilitate synaptic plasticity" @default.
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- W2884299905 doi "https://doi.org/10.1038/s41593-018-0184-3" @default.
- W2884299905 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6100743" @default.
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