A mechanism underlying AMPA receptor trafficking during cerebellar long-term potentiation

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Abstract

Long-term potentiation (LTP) is mediated by the activity-driven delivery of GluR1 glutamate receptors via Ca2+/calmodulin-dependent protein kinase II activity in various brain regions. Recently, postsynaptic LTP was shown to be induced at parallel fiber-Purkinje cell synapses by stimulating the parallel fibers at 1 Hz or applying a NO donor. Here, we demonstrate that NO-evoked postsynaptic LTP in mice cerebellum was blocked by botulinum toxin and enhanced by prior treatment with phorbol ester, which is known to induce GluR2 endocytosis. Interestingly, such LTP was not affected by a Ca 2+/calmodulin-dependent protein kinase II inhibitor or a peptide binding to a protein interacting with C kinase 1, but was blocked by a peptide binding to N-ethylmaleimide-sensitive factor, which specifically binds to GluR2. Therefore, although the synaptic incorporation of GluR2 has been reported to be a constitutive pathway, NO-induced postsynaptic LTP in Purkinje cells is likely mediated by a pathway involving N-ethylmaleimide-sensitive factor-dependent GluR2 trafficking.

Original languageEnglish
Pages (from-to)17846-17851
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume102
Issue number49
DOIs
Publication statusPublished - 2005 Dec 6

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AMPA Receptors
Long-Term Potentiation
N-Ethylmaleimide-Sensitive Proteins
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Purkinje Cells
Calcium-Calmodulin-Dependent Protein Kinases
Peptides
Botulinum Toxins
Glutamate Receptors
Phorbol Esters
Protein Kinase Inhibitors
Endocytosis
Synapses
Cerebellum
Phosphotransferases
Brain
Proteins

Keywords

  • Cerebellum
  • Glutamate receptor
  • Long-term depression
  • Nitric oxide

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

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title = "A mechanism underlying AMPA receptor trafficking during cerebellar long-term potentiation",
abstract = "Long-term potentiation (LTP) is mediated by the activity-driven delivery of GluR1 glutamate receptors via Ca2+/calmodulin-dependent protein kinase II activity in various brain regions. Recently, postsynaptic LTP was shown to be induced at parallel fiber-Purkinje cell synapses by stimulating the parallel fibers at 1 Hz or applying a NO donor. Here, we demonstrate that NO-evoked postsynaptic LTP in mice cerebellum was blocked by botulinum toxin and enhanced by prior treatment with phorbol ester, which is known to induce GluR2 endocytosis. Interestingly, such LTP was not affected by a Ca 2+/calmodulin-dependent protein kinase II inhibitor or a peptide binding to a protein interacting with C kinase 1, but was blocked by a peptide binding to N-ethylmaleimide-sensitive factor, which specifically binds to GluR2. Therefore, although the synaptic incorporation of GluR2 has been reported to be a constitutive pathway, NO-induced postsynaptic LTP in Purkinje cells is likely mediated by a pathway involving N-ethylmaleimide-sensitive factor-dependent GluR2 trafficking.",
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author = "Wataru Kakegawa and Michisuke Yuzaki",
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AU - Kakegawa, Wataru

AU - Yuzaki, Michisuke

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N2 - Long-term potentiation (LTP) is mediated by the activity-driven delivery of GluR1 glutamate receptors via Ca2+/calmodulin-dependent protein kinase II activity in various brain regions. Recently, postsynaptic LTP was shown to be induced at parallel fiber-Purkinje cell synapses by stimulating the parallel fibers at 1 Hz or applying a NO donor. Here, we demonstrate that NO-evoked postsynaptic LTP in mice cerebellum was blocked by botulinum toxin and enhanced by prior treatment with phorbol ester, which is known to induce GluR2 endocytosis. Interestingly, such LTP was not affected by a Ca 2+/calmodulin-dependent protein kinase II inhibitor or a peptide binding to a protein interacting with C kinase 1, but was blocked by a peptide binding to N-ethylmaleimide-sensitive factor, which specifically binds to GluR2. Therefore, although the synaptic incorporation of GluR2 has been reported to be a constitutive pathway, NO-induced postsynaptic LTP in Purkinje cells is likely mediated by a pathway involving N-ethylmaleimide-sensitive factor-dependent GluR2 trafficking.

AB - Long-term potentiation (LTP) is mediated by the activity-driven delivery of GluR1 glutamate receptors via Ca2+/calmodulin-dependent protein kinase II activity in various brain regions. Recently, postsynaptic LTP was shown to be induced at parallel fiber-Purkinje cell synapses by stimulating the parallel fibers at 1 Hz or applying a NO donor. Here, we demonstrate that NO-evoked postsynaptic LTP in mice cerebellum was blocked by botulinum toxin and enhanced by prior treatment with phorbol ester, which is known to induce GluR2 endocytosis. Interestingly, such LTP was not affected by a Ca 2+/calmodulin-dependent protein kinase II inhibitor or a peptide binding to a protein interacting with C kinase 1, but was blocked by a peptide binding to N-ethylmaleimide-sensitive factor, which specifically binds to GluR2. Therefore, although the synaptic incorporation of GluR2 has been reported to be a constitutive pathway, NO-induced postsynaptic LTP in Purkinje cells is likely mediated by a pathway involving N-ethylmaleimide-sensitive factor-dependent GluR2 trafficking.

KW - Cerebellum

KW - Glutamate receptor

KW - Long-term depression

KW - Nitric oxide

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