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Neuron. 2018 Mar 7;97(5):1110-1125.e14. doi: 10.1016/j.neuron.2018.01.046. Epub 2018 Feb 22.

Caldendrin Directly Couples Postsynaptic Calcium Signals to Actin Remodeling in Dendritic Spines.

Author information

1
Emmy Noether Group "Neuronal Protein Transport," Center for Molecular Neurobiology, ZMNH, University Medical Center Hamburg-Eppendorf, Hamburg 20251, Germany; RG Neuroplasticity, Leibniz-Institute for Neurobiology, Magdeburg 39118, Germany; Cell Biology, Faculty of Science, Utrecht University, Utrecht 3584 CH, the Netherlands. Electronic address: marina.mikhaylova@zmnh.uni-hamburg.de.
2
Emmy Noether Group "Neuronal Protein Transport," Center for Molecular Neurobiology, ZMNH, University Medical Center Hamburg-Eppendorf, Hamburg 20251, Germany; RG Neuroplasticity, Leibniz-Institute for Neurobiology, Magdeburg 39118, Germany.
3
Emmy Noether Group "Neuronal Protein Transport," Center for Molecular Neurobiology, ZMNH, University Medical Center Hamburg-Eppendorf, Hamburg 20251, Germany.
4
Cell Biology, Faculty of Science, Utrecht University, Utrecht 3584 CH, the Netherlands.
5
RG Neuroplasticity, Leibniz-Institute for Neurobiology, Magdeburg 39118, Germany.
6
State Lab for Photon Energetics, Bauman Moscow State University, Moscow 105005, Russia.
7
Combinatorial Neuroimaging Core Facility (CNI), Leibniz Institute for Neurobiology, Magdeburg 39118, Germany.
8
Institute of Biology, Otto von Guericke University, Magdeburg 39120, Germany.
9
RG Neuroplasticity, Leibniz-Institute for Neurobiology, Magdeburg 39118, Germany; Leibniz Group "Dendritic Organelles and Synaptic Function," Center for Molecular Neurobiology, ZMNH, University Medical Center Hamburg-Eppendorf, Hamburg 20251, Germany. Electronic address: michael.kreutz@lin-magdeburg.de.

Abstract

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.

KEYWORDS:

F-actin; STED; calcium; caldendrin; cofilin; cortactin; dendritic spines; synaptic plasticity

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