Cerebellar Long-Term Depression Requires PKC-Regulated Interactions between GluR2/3 and PDZ Domain–Containing Proteins
pmid: 11144359
Cerebellar Long-Term Depression Requires PKC-Regulated Interactions between GluR2/3 and PDZ Domain–Containing Proteins
Cerebellar LTD requires activation of PKC and is expressed, at least in part, as postsynaptic AMPA receptor internalization. Recently, it was shown that AMPA receptor internalization requires clathrin-mediated endocytosis and depends upon the carboxy-terminal region of GluR2/3. Phosphorylation of Ser-880 in this region by PKC differentially regulates the binding of the PDZ domain-containing proteins GRIP/ABP and PICK1. Peptides, corresponding to the phosphorylated and dephosphorylated GluR2 carboxy-terminal PDZ binding motif, were perfused in cerebellar Purkinje cells grown in culture. Both the dephospho form (which blocks binding of GRIP/ABP and PICK1) and the phospho form (which selectively blocks PICK1) attenuated LTD induction by glutamate/depolarization pairing, as did antibodies directed against the PDZ domain of PICK1. These findings indicate that expression of cerebellar LTD requires PKC-regulated interactions between the carboxy-terminal of GluR2/3 and PDZ domain-containing proteins.
- Hong Kong Polytechnic University China (People's Republic of)
- Johns Hopkins Medicine United States
- Johns Hopkins University School of Medicine United States
- Hong Kong University of Science and Technology (香港科技大學) China (People's Republic of)
- Department of Neuroscience Italy
570, Neuronal Plasticity, Patch-Clamp Techniques, Neuroscience(all), Amino Acid Motifs, Excitatory Postsynaptic Potentials, Nuclear Proteins, Cell Cycle Proteins, Nerve Tissue Proteins, Neural Inhibition, Binding, Competitive, Antibodies, Peptide Fragments, Mice, Cerebellum, Animals, Calcium, Phosphorylation, Carrier Proteins, Cells, Cultured, Protein Kinase C, Adaptor Proteins, Signal Transducing
570, Neuronal Plasticity, Patch-Clamp Techniques, Neuroscience(all), Amino Acid Motifs, Excitatory Postsynaptic Potentials, Nuclear Proteins, Cell Cycle Proteins, Nerve Tissue Proteins, Neural Inhibition, Binding, Competitive, Antibodies, Peptide Fragments, Mice, Cerebellum, Animals, Calcium, Phosphorylation, Carrier Proteins, Cells, Cultured, Protein Kinase C, Adaptor Proteins, Signal Transducing
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