Organization and dynamics of the actin cytoskeleton during dendritic spine morphological remodeling

被引:60
作者
Chazeau, Anael [1 ,2 ,3 ]
Giannone, Gregory [1 ,2 ]
机构
[1] Univ Bordeaux, Interdisciplinary Inst Neurosci, UMR 5297, F-33000 Bordeaux, France
[2] CNRS, Interdisciplinary Inst Neurosci, UMR 5297, F-33000 Bordeaux, France
[3] Univ Utrecht, Cell Biol, Fac Sci, Padualaan 8, NL-3584 CH Utrecht, Netherlands
关键词
Dendritic spines; Actin cytoskeleton; Actin binding proteins; PSD; CAMKII; Synaptic plasticity; Super-resolution microscopy; LONG-TERM POTENTIATION; AMPA-RECEPTOR TRAFFICKING; CULTURED HIPPOCAMPAL-NEURONS; FILAMENT-BINDING PROTEIN; LIGHT-SHEET MICROSCOPY; N-CADHERIN ADHESIONS; LIVING BRAIN-SLICES; SYNAPTIC PLASTICITY; ARP2/3; COMPLEX; POSTSYNAPTIC DENSITY;
D O I
10.1007/s00018-016-2214-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In the central nervous system, most excitatory post-synapses are small subcellular structures called dendritic spines. Their structure and morphological remodeling are tightly coupled to changes in synaptic transmission. The F-actin cytoskeleton is the main driving force of dendritic spine remodeling and sustains synaptic plasticity. It is therefore essential to understand how changes in synaptic transmission can regulate the organization and dynamics of actin binding proteins (ABPs). In this review, we will provide a detailed description of the organization and dynamics of F-actin and ABPs in dendritic spines and will discuss the current models explaining how the actin cytoskeleton sustains both structural and functional synaptic plasticity.
引用
收藏
页码:3053 / 3073
页数:21
相关论文
共 302 条
[1]   A "Primer"-Based Mechanism Underlies Branched Actin Filament Network Formation and Motility [J].
Achard, Verane ;
Martiel, Jean-Louis ;
Michelot, Alphee ;
Guerin, Christophe ;
Reymann, Anne-Cecile ;
Blanchoin, Laurent ;
Boujemaa-Paterski, Rajaa .
CURRENT BIOLOGY, 2010, 20 (05) :423-428
[2]   Activity-induced targeting of profilin and stabilization of dendritic spine morphology [J].
Ackermann, M ;
Matus, A .
NATURE NEUROSCIENCE, 2003, 6 (11) :1194-1200
[3]   Barriers in the brain: resolving dendritic spine morphology and compartmentalization [J].
Adrian, Max ;
Kusters, Remy ;
Wierenga, Corette J. ;
Storm, Cornelis ;
Hoogenraad, Casper C. ;
Kapitein, Lukas C. .
FRONTIERS IN NEUROANATOMY, 2014, 8
[4]  
Ahrens MB, 2013, NAT METHODS, V10, P413, DOI [10.1038/NMETH.2434, 10.1038/nmeth.2434]
[5]  
Allison DW, 1998, J NEUROSCI, V18, P2423
[6]   Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy [J].
Amann, KJ ;
Pollard, TD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (26) :15009-15013
[7]   Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin [J].
Andrianantoandro, Ernesto ;
Pollard, Thomas D. .
MOLECULAR CELL, 2006, 24 (01) :13-23
[8]   Regulation of AMPA receptor trafficking and synaptic plasticity [J].
Anggono, Victor ;
Huganir, Richard L. .
CURRENT OPINION IN NEUROBIOLOGY, 2012, 22 (03) :461-469
[9]   Drebrin A is a postsynaptic protein that localizes in vivo to the submembranous surface of dendritic sites forming excitatory synapses [J].
Aoki, C ;
Sekino, Y ;
Hanamura, K ;
Fujisawa, S ;
Mahadomrongkul, V ;
Ren, Y ;
Shirao, T .
JOURNAL OF COMPARATIVE NEUROLOGY, 2005, 483 (04) :383-402
[10]   Regulation of hippocampal long-term potentiation by p21-activated protein kinase 1 (PAK1) [J].
Asrar, Suhail ;
Meng, Yanghong ;
Zhou, Zikai ;
Todorovski, Zarko ;
Huang, Wayne Wenyin ;
Jia, Zhengping .
NEUROPHARMACOLOGY, 2009, 56 (01) :73-80