scholarly journals Neocortical Long-Term Potentiation and Experience-Dependent Synaptic Plasticity Require α-Calcium/Calmodulin-Dependent Protein Kinase II Autophosphorylation

2003 ◽  
Vol 23 (11) ◽  
pp. 4428-4436 ◽  
Author(s):  
Neil Hardingham ◽  
Stanislaw Glazewski ◽  
Pavel Pakhotin ◽  
Keiko Mizuno ◽  
Paul F. Chapman ◽  
...  
Keyword(s):  
Synaptic Plasticity ◽  
Protein Kinase ◽  
Long Term Potentiation ◽  
Dependent Protein Kinase ◽  
Calcium Calmodulin Dependent ◽  
Term Potentiation ◽  
Protein Kinase Ii ◽  
Dependent Protein

AMPA receptor phosphorylation during synaptic plasticity

2005 ◽  
Vol 33 (6) ◽  
pp. 1354-1356 ◽  
Author(s):  
J. Boehm ◽  
R. Malinow
Keyword(s):  
Protein Kinase ◽  
Long Term Potentiation ◽  
Synaptic Activity ◽  
Dependent Protein Kinase ◽  
Enhanced Transmission ◽  
Calcium Calmodulin Dependent ◽  
Term Potentiation ◽  
Dependent Protein ◽  
Biochemical Analyses

A widely studied example of vertebrate plasticity is LTP (long-term potentiation), the persistent synaptic enhancement that follows a brief period of coinciding pre- and post-synaptic activity. During LTP, different kinases, including CaMKII (calcium/calmodulin-dependent protein kinase II) and protein kinase A, become activated and play critical roles in induction and maintenance of enhanced transmission. Biochemical analyses have revealed several regulated phosphorylation sites in the AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor subunits, GluR1 and GluR4. The regulated insertion of these receptors is a key event in the induction of LTP. Here, we discuss the phosphorylation of GluR1 and GluR4 and its role in receptor delivery and neuronal plasticity.

Ca2+/calmodulin-dependent protein kinase II-dependent long-term potentiation in the rat suprachiasmatic nucleus and its inhibition by melatonin

2002 ◽  
Vol 70 (6) ◽  
pp. 799-807 ◽  
Author(s):  
Kohji Fukunaga ◽  
Kazumasa Horikawa ◽  
Shigenobu Shibata ◽  
Yusuke Takeuchi ◽  
Eishichi Miyamoto
Keyword(s):  
Protein Kinase ◽  
Suprachiasmatic Nucleus ◽  
Long Term Potentiation ◽  
Dependent Protein Kinase ◽  
Term Potentiation ◽  
Protein Kinase Ii ◽  
Dependent Protein

Amyloid β Prevents Activation of Calcium/Calmodulin-Dependent Protein Kinase II and AMPA Receptor Phosphorylation During Hippocampal Long-Term Potentiation

2004 ◽  
Vol 92 (5) ◽  
pp. 2853-2858 ◽  
Author(s):  
Danyun Zhao ◽  
Joseph B. Watson ◽  
Cui-Wei Xie
Keyword(s):  
Synaptic Plasticity ◽  
Protein Kinase ◽  
Amyloid Β ◽  
Long Term Potentiation ◽  
Perforant Path ◽  
Dependent Protein Kinase ◽  
Term Potentiation ◽  
Dependent Protein ◽  
Dependent Site

Accumulation of amyloid β-peptides (Aβ) in the brain has been linked with memory loss in Alzheimer's disease and its animal models. However, the synaptic mechanism by which Aβ causes memory deficits remains unclear. We previously showed that acute application of Aβ inhibited long-term potentiation (LTP) in the hippocampal perforant path via activation of calcineurin, a Ca2+-dependent protein phosphatase. This study examined whether Aβ could also inhibit Ca2+/calmodulin dependent protein kinase II (CaMKII), further disrupting the dynamic balance between protein kinase and phosphatase during synaptic plasticity. Immunoblot analysis was conducted to measure autophosphorylation of CaMKII at Thr286 and phosphorylation of the GluR1 subunit of AMPA receptors in single rat hippocampal slices. A high-frequency tetanus applied to the perforant path significantly increased CaMKII autophosphorylation and subsequent phosphorylation of GluR1 at Ser831, a CaMKII-dependent site, in the dentate area. Acute application of Aβ1–42 inhibited dentate LTP and associated phosphorylation processes, but was without effect on phosphorylation of GluR1 at Ser845, a protein kinase A-dependent site. These results suggest that activity-dependent CaMKII autophosphorylation and AMPA receptor phosphorylation are essential for dentate LTP. Disruption of such mechanisms could directly contribute to Aβ-induced deficits in hippocampal synaptic plasticity and memory.

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