Caldendrin Directly Couples Postsynaptic Calcium Signals to Actin Remodeling in Dendritic Spines
| Autor: | Anja Konietzny, Jeffrey Lopez-Rojas, Julia Bär, Michael R. Kreutz, Oliver Stork, Bas van Bommel, Marina Mikhaylova, Egor Y. Loktionov, Syed Ahsan Raza, Casper C. Hoogenraad, Pasham Parameshwar Reddy, Oliver Kobler, Rajeev Raman, Philipp Schätzle, Johannes Hradsky, Christina Spilker, PingAn Yuanxiang |
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| Přispěvatelé: | Sub Cell Biology, Celbiologie |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Dendritic spine Dendritic Spines Long-Term Potentiation cofilin macromolecular substances Filamentous actin Hippocampus F-actin 03 medical and health sciences Mice Organ Culture Techniques Postsynaptic potential Chlorocebus aethiops Animals Humans Calcium Signaling Rats Wistar Cells Cultured Mice Knockout calcium synaptic plasticity biology Chemistry General Neuroscience Calcium-Binding Proteins Actin remodeling Long-term potentiation dendritic spines cortactin Cofilin Synaptic Potentials caldendrin Cell biology Rats STED Mice Inbred C57BL 030104 developmental biology HEK293 Cells Synaptic plasticity COS Cells biology.protein Cortactin |
| Zdroj: | Neuron, 97(5), 1110. Cell Press Neuron |
| ISSN: | 1097-4199 0896-6273 |
| Popis: | Compartmentalization of calcium-dependent plasticity allows for rapid actin remodeling in dendritic spines. However, molecular mechanisms for the spatio-temporal regulation of filamentous actin (F-actin) dynamics by spinous Ca2+-transients are still poorly defined. We show that the postsynaptic Ca2+ sensor caldendrin orchestrates nano-domain actin dynamics that are essential for actin remodeling in the early phase of long-term potentiation (LTP). Steep elevation in spinous [Ca2+]i disrupts an intramolecular interaction of caldendrin and allows cortactin binding. The fast on and slow off rate of this interaction keeps cortactin in an active conformation, and protects F-actin at the spine base against cofilin-induced severing. Caldendrin gene knockout results in higher synaptic actin turnover, altered nanoscale organization of spinous F-actin, defects in structural spine plasticity, LTP, and hippocampus-dependent learning. Collectively, the data indicate that caldendrin-cortactin directly couple [Ca2+]i to preserve a minimal F-actin pool that is required for actin remodeling in the early phase of LTP. |
| Databáze: | OpenAIRE |
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