PortalPublikationenCaldendrin Directly Couples Postsynaptic Calcium Signals to ...

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

Standard

Caldendrin Directly Couples Postsynaptic Calcium Signals to Actin Remodeling in Dendritic Spines. / Mikhaylova, Marina; Bär, Julia; van Bommel, Bas; Schätzle, Philipp; YuanXiang, PingAn; Raman, Rajeev; Hradsky, Johannes; Konietzny, Anja; Loktionov, Egor Y; Reddy, Pasham Parameshwar; Lopez-Rojas, Jeffrey; Spilker, Christina; Kobler, Oliver; Raza, Syed Ahsan; Stork, Oliver; Hoogenraad, Casper C; Kreutz, Michael R.

in: NEURON, Jahrgang 97, Nr. 5, 07.03.2018, S. 1110-1125.e14.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Mikhaylova, M, Bär, J, van Bommel, B, Schätzle, P, YuanXiang, P, Raman, R, Hradsky, J, Konietzny, A, Loktionov, EY, Reddy, PP, Lopez-Rojas, J, Spilker, C, Kobler, O, Raza, SA, Stork, O, Hoogenraad, CC & Kreutz, MR 2018, 'Caldendrin Directly Couples Postsynaptic Calcium Signals to Actin Remodeling in Dendritic Spines', NEURON, Jg. 97, Nr. 5, S. 1110-1125.e14. https://doi.org/10.1016/j.neuron.2018.01.046

APA

Mikhaylova, M., Bär, J., van Bommel, B., Schätzle, P., YuanXiang, P., Raman, R., Hradsky, J., Konietzny, A., Loktionov, E. Y., Reddy, P. P., Lopez-Rojas, J., Spilker, C., Kobler, O., Raza, S. A., Stork, O., Hoogenraad, C. C., & Kreutz, M. R. (2018). Caldendrin Directly Couples Postsynaptic Calcium Signals to Actin Remodeling in Dendritic Spines. NEURON, 97(5), 1110-1125.e14. https://doi.org/10.1016/j.neuron.2018.01.046

Vancouver

Mikhaylova M, Bär J, van Bommel B, Schätzle P, YuanXiang P, Raman R et al. Caldendrin Directly Couples Postsynaptic Calcium Signals to Actin Remodeling in Dendritic Spines. NEURON. 2018 Mär 7;97(5):1110-1125.e14. https://doi.org/10.1016/j.neuron.2018.01.046

Bibtex

@article{5dc62dfae9384269aab0cb08a775c110,
title = "Caldendrin Directly Couples Postsynaptic Calcium Signals to Actin Remodeling in Dendritic Spines",
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+]idisrupts 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+]ito preserve a minimal F-actin pool that is required for actin remodeling in the early phase of LTP.",
keywords = "Journal Article",
author = "Marina Mikhaylova and Julia B{\"a}r and {van Bommel}, Bas and Philipp Sch{\"a}tzle and PingAn YuanXiang and Rajeev Raman and Johannes Hradsky and Anja Konietzny and Loktionov, {Egor Y} and Reddy, {Pasham Parameshwar} and Jeffrey Lopez-Rojas and Christina Spilker and Oliver Kobler and Raza, {Syed Ahsan} and Oliver Stork and Hoogenraad, {Casper C} and Kreutz, {Michael R}",
note = "Copyright {\textcopyright} 2018 Elsevier Inc. All rights reserved.",
year = "2018",
month = mar,
day = "7",
doi = "10.1016/j.neuron.2018.01.046",
language = "English",
volume = "97",
pages = "1110--1125.e14",
journal = "NEURON",
issn = "0896-6273",
publisher = "Cell Press",
number = "5",

}

RIS

TY - JOUR

T1 - Caldendrin Directly Couples Postsynaptic Calcium Signals to Actin Remodeling in Dendritic Spines

AU - Mikhaylova, Marina

AU - Bär, Julia

AU - van Bommel, Bas

AU - Schätzle, Philipp

AU - YuanXiang, PingAn

AU - Raman, Rajeev

AU - Hradsky, Johannes

AU - Konietzny, Anja

AU - Loktionov, Egor Y

AU - Reddy, Pasham Parameshwar

AU - Lopez-Rojas, Jeffrey

AU - Spilker, Christina

AU - Kobler, Oliver

AU - Raza, Syed Ahsan

AU - Stork, Oliver

AU - Hoogenraad, Casper C

AU - Kreutz, Michael R

N1 - Copyright © 2018 Elsevier Inc. All rights reserved.

PY - 2018/3/7

Y1 - 2018/3/7

N2 - 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+]idisrupts 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+]ito preserve a minimal F-actin pool that is required for actin remodeling in the early phase of LTP.

AB - 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+]idisrupts 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+]ito preserve a minimal F-actin pool that is required for actin remodeling in the early phase of LTP.

KW - Journal Article

U2 - 10.1016/j.neuron.2018.01.046

DO - 10.1016/j.neuron.2018.01.046

M3 - SCORING: Journal article

C2 - 29478916

VL - 97

SP - 1110-1125.e14

JO - NEURON

JF - NEURON

SN - 0896-6273

IS - 5

ER -