Protein kinase C in synaptic plasticity: changes in the in situ phosphorylation state of identified pre- and postsynaptic substrates.
1. Long-term potentiation and its counterpart long-term depression are two forms of activity dependent synaptic plasticity, in which protein kinases and protein phosphatases are essential. 2. B-50/GAP-43 and RC3/neurogranin are two defined neuronal PKC substrates with different synaptic localization. B-50/GAP-43 is a presynaptic protein and RC3/neurogranin is only found at the postsynaptic site. Measuring their phosphorylation state in hippocampal slices, allows us to simultaneously monitor changes in pre- and postsynaptic PKC mediated phosphorylation. 3. Induction of LTP in the CA1 field of the hippocampus is accompanied with an increase in the in situ phosphorylation of both B-50/GAP-43 and RC3/neurogranin, during narrow, partially overlapping, time windows. 4. Pharmacological data show that mGluR stimulation results in an increase in the in situ phosphorylation of B-50/GAP-43 and RC3/neurogranin.
Ramakers
G M
GM
Rudolf Magnus Institute for Neurosciences, Utrecht, The Netherlands.
Pasinelli
P
P
Hens
J J
JJ
Gispen
W H
WH
De Graan
P N
PN
D000818:Animals; D006624:Hippocampus / Q000502:physiology*; D017774:Long-Term Potentiation / Q000502:physiology; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009473:Neuronal Plasticity / Q000502:physiology*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism; D013379:Substrate Specificity; D013569:Synapses / Q000502:physiology*
D009419:Nerve Tissue Proteins; D011494:Protein Kinases; D011493:Protein Kinase C; D010749:Phosphoprotein Phosphatases