scholarly journals Decreased calcium/calmodulin-dependent protein kinase II and protein kinase C activities mediate impairment of hippocampal long-term potentiation in the olfactory bulbectomized mice

2006 ◽  
Vol 97 (1) ◽  
pp. 22-29 ◽  
Author(s):  
Shigeki Moriguchi ◽  
Feng Han ◽  
Osamu Nakagawasai ◽  
Takeshi Tadano ◽  
Kohji Fukunaga
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Long Term Potentiation ◽  
Dependent Protein Kinase ◽  
Calcium Calmodulin Dependent ◽  
Kinase C ◽  
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.

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