Developmentally regulated changes in cellular compartmentation and synaptic distribution of actin in hippocampal neurons

2002 ◽  
Vol 69 (4) ◽  
pp. 427-436 ◽  
Author(s):  
Wandong Zhang ◽  
Deanna L. Benson
2019 ◽  
Vol 12 (586) ◽  
pp. eaav3577 ◽  
Author(s):  
Pedro Afonso ◽  
Pasqualino De Luca ◽  
Rafael S. Carvalho ◽  
Luísa Cortes ◽  
Paulo Pinheiro ◽  
...  

The effects of brain-derived neurotrophic factor (BDNF) in long-term synaptic potentiation (LTP) are thought to underlie learning and memory formation and are partly mediated by local protein synthesis. Here, we investigated the mechanisms that mediate BDNF-induced alterations in the synaptic proteome that are coupled to synaptic strengthening. BDNF induced the synaptic accumulation of GluN2B-containing NMDA receptors (NMDARs) and increased the amplitude of NMDAR-mediated miniature excitatory postsynaptic currents (mEPSCs) in cultured rat hippocampal neurons by a mechanism requiring activation of the protein tyrosine kinase Pyk2 and dependent on cellular protein synthesis. Single-particle tracking using quantum dot imaging revealed that the increase in the abundance of synaptic NMDAR currents correlated with their enhanced stability in the synaptic compartment. Furthermore, BDNF increased the local synthesis of Pyk2 at the synapse, and the observed increase in Pyk2 protein abundance along dendrites of cultured hippocampal neurons was mediated by a mechanism dependent on the ribonucleoprotein hnRNP K, which bound to Pyk2 mRNA and dissociated from it upon BDNF application. Knocking down hnRNP K reduced the BDNF-induced synaptic synthesis of Pyk2 protein, whereas its overexpression enhanced it. Together, these findings indicate that hnRNP K mediates the synaptic distribution of Pyk2 synthesis, and hence the synaptic incorporation of GluN2B-containing NMDARs, induced by BDNF, which may affect LTP and synaptic plasticity.


2007 ◽  
Vol 178 (3) ◽  
pp. 489-502 ◽  
Author(s):  
Mian Xie ◽  
Xiang Li ◽  
Jing Han ◽  
Daniel L. Vogt ◽  
Silke Wittemann ◽  
...  

Ca2+ channel β subunits determine the transport and physiological properties of high voltage–activated Ca2+ channel complexes. Our analysis of the distribution of the Cavβ subunit family members in hippocampal neurons correlates their synaptic distribution with their involvement in transmitter release. We find that exogenously expressed Cavβ4b and Cavβ2a subunits distribute in clusters and localize to synapses, whereas Cavβ1b and Cavβ3 are homogenously distributed. According to their localization, Cavβ2a and Cavβ4b subunits modulate the synaptic plasticity of autaptic hippocampal neurons (i.e., Cavβ2a induces depression, whereas Cavβ4b induces paired-pulse facilitation [PPF] followed by synaptic depression during longer stimuli trains). The induction of PPF by Cavβ4b correlates with a reduction in the release probability and cooperativity of the transmitter release. These results suggest that Cavβ subunits determine the gating properties of the presynaptic Ca2+ channels within the presynaptic terminal in a subunit-specific manner and may be involved in organization of the Ca2+ channel relative to the release machinery.


2002 ◽  
Vol 157 (7) ◽  
pp. 1197-1209 ◽  
Author(s):  
Pascal Steiner ◽  
J.-C. Floyd Sarria ◽  
Liliane Glauser ◽  
Sarah Magnin ◽  
Stefan Catsicas ◽  
...  

Although correct cycling of neuronal membrane proteins is essential for neurite outgrowth and synaptic plasticity, neuron-specific proteins of the implicated endosomes have not been characterized. Here we show that a previously cloned, developmentally regulated, neuronal protein of unknown function binds to syntaxin 13. We propose to name this protein neuron-enriched endosomal protein of 21 kD (NEEP21), because it is colocalized with transferrin receptors, internalized transferrin (Tf), and Rab4. In PC12 cells, NEEP21 overexpression accelerates Tf internalization and recycling, whereas its down-regulation strongly delays Tf recycling. In primary neurons, NEEP21 is localized to the somatodendritic compartment, and, upon N-methyl-d-aspartate (NMDA) stimulation, the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate receptor subunit GluR2 is internalized into NEEP21-positive endosomes. NEEP21 down-regulation retards recycling of GluR1 to the cell surface after NMDA stimulation of hippocampal neurons. In summary, NEEP21 is a neuronal protein that is localized to the early endosomal pathway and is necessary for correct receptor recycling in neurons.


2005 ◽  
Vol 30 (3) ◽  
pp. 304-315 ◽  
Author(s):  
Cristian Galvan ◽  
Paola G. Camoletto ◽  
Carlos G. Dotti ◽  
Adriano Aguzzi ◽  
Maria Dolores Ledesma

Development ◽  
1992 ◽  
Vol 115 (3) ◽  
pp. 885-892 ◽  
Author(s):  
P. Doherty ◽  
S.D. Skaper ◽  
S.E. Moore ◽  
A. Leon ◽  
F.S. Walsh

Monolayers of control 3T3 fibroblasts and 3T3 cells expressing transfected NCAM or N-cadherin have been used as a culture substratum for rat hippocampal neurons. Both NCAM and N-cadherin are expressed in the hippocampus through embryonic day 17 (E17) to postnatal day 4 (PND4); however, whereas E17 neurons responded to transfected NCAM by extending considerably longer neurites, PND4 neurons responded very poorly. The converse was true for responsiveness to N-cadherin. These data demonstrate a switch in neuronal responsiveness to NCAM and N-cadherin in the developing hippocampus. NCAM-dependent neurite outgrowth from E17 neurons was largely dependent on the presence of alpha 2–8-linked polysialic acid (PSA) on neuronal NCAM. NCAM-dependent neurite outgrowth could be fully inhibited by pertussis toxin or a combination of L- and N-type calcium channel antagonists thus providing direct evidence concerning the nature of the second messenger pathway activated in primary neurons by cell adhesion molecules (CAMs).


2015 ◽  
Vol 41 (1-2) ◽  
pp. 290-297 ◽  
Author(s):  
Karen Siaw-Ling Wee ◽  
Francis Chee Kuan Tan ◽  
Yoke-Ping Cheong ◽  
Sanjay Khanna ◽  
Chian-Ming Low

2010 ◽  
Vol 34 (8) ◽  
pp. S74-S74
Author(s):  
Tingyu Li ◽  
Xiaojuan Zhang ◽  
Xuan Zhang ◽  
Jian Hea ◽  
Yang Bi Youxue Liu ◽  
...  

1999 ◽  
Vol 19 (3) ◽  
pp. 302-310
Author(s):  
Yukihiko Kohda ◽  
Katsuhiro Tsuchiya ◽  
Junkoh Yamashita ◽  
Masaki Yoshida ◽  
Takashi Ueno ◽  
...  

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