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The Availability of Surface GABAB Receptors Is Independent of γ-Aminobutyric Acid but Controlled by Glutamate in Central Neurons
The efficacy of synaptic transmission depends on the availability of ionotropic and metabotropic neurotransmitter receptors at the plasma membrane, but the contribution of the endocytic and recycling pathways in the regulation of γ-aminobutyric acid type B (GABA B ) receptors remains controversial....
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Published in: | The Journal of biological chemistry 2008-09, Vol.283 (36), p.24641 |
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container_issue | 36 |
container_start_page | 24641 |
container_title | The Journal of biological chemistry |
container_volume | 283 |
creator | Karina J. Vargas Miho Terunuma Judith A. Tello Menelas N. Pangalos Stephen J. Moss Andrés Couve |
description | The efficacy of synaptic transmission depends on the availability of ionotropic and metabotropic neurotransmitter receptors
at the plasma membrane, but the contribution of the endocytic and recycling pathways in the regulation of γ-aminobutyric acid
type B (GABA B ) receptors remains controversial. To understand the mechanisms that regulate the abundance of GABA B receptors, we have studied their turnover combining surface biotin labeling and a microscopic immunoendocytosis assay in
hippocampal and cortical neurons. We report that internalization of GABA B receptors is agonist-independent. We also demonstrate that receptors endocytose in the cell body and dendrites but not in
axons. Additionally, we show that GABA B receptors endocytose as heterodimers via clathrin- and dynamin-1-dependent mechanisms and that they recycle to the plasma
membrane after endocytosis. More importantly, we show that glutamate decreases the levels of cell surface receptors in a manner
dependent on an intact proteasome pathway. These observations indicate that glutamate and not GABA controls the abundance
of surface GABA B receptors in central neurons, consistent with their enrichment at glutamatergic synapses. |
doi_str_mv | 10.1074/jbc.M802419200 |
format | article |
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at the plasma membrane, but the contribution of the endocytic and recycling pathways in the regulation of γ-aminobutyric acid
type B (GABA B ) receptors remains controversial. To understand the mechanisms that regulate the abundance of GABA B receptors, we have studied their turnover combining surface biotin labeling and a microscopic immunoendocytosis assay in
hippocampal and cortical neurons. We report that internalization of GABA B receptors is agonist-independent. We also demonstrate that receptors endocytose in the cell body and dendrites but not in
axons. Additionally, we show that GABA B receptors endocytose as heterodimers via clathrin- and dynamin-1-dependent mechanisms and that they recycle to the plasma
membrane after endocytosis. More importantly, we show that glutamate decreases the levels of cell surface receptors in a manner
dependent on an intact proteasome pathway. These observations indicate that glutamate and not GABA controls the abundance
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at the plasma membrane, but the contribution of the endocytic and recycling pathways in the regulation of γ-aminobutyric acid
type B (GABA B ) receptors remains controversial. To understand the mechanisms that regulate the abundance of GABA B receptors, we have studied their turnover combining surface biotin labeling and a microscopic immunoendocytosis assay in
hippocampal and cortical neurons. We report that internalization of GABA B receptors is agonist-independent. We also demonstrate that receptors endocytose in the cell body and dendrites but not in
axons. Additionally, we show that GABA B receptors endocytose as heterodimers via clathrin- and dynamin-1-dependent mechanisms and that they recycle to the plasma
membrane after endocytosis. More importantly, we show that glutamate decreases the levels of cell surface receptors in a manner
dependent on an intact proteasome pathway. These observations indicate that glutamate and not GABA controls the abundance
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at the plasma membrane, but the contribution of the endocytic and recycling pathways in the regulation of γ-aminobutyric acid
type B (GABA B ) receptors remains controversial. To understand the mechanisms that regulate the abundance of GABA B receptors, we have studied their turnover combining surface biotin labeling and a microscopic immunoendocytosis assay in
hippocampal and cortical neurons. We report that internalization of GABA B receptors is agonist-independent. We also demonstrate that receptors endocytose in the cell body and dendrites but not in
axons. Additionally, we show that GABA B receptors endocytose as heterodimers via clathrin- and dynamin-1-dependent mechanisms and that they recycle to the plasma
membrane after endocytosis. More importantly, we show that glutamate decreases the levels of cell surface receptors in a manner
dependent on an intact proteasome pathway. These observations indicate that glutamate and not GABA controls the abundance
of surface GABA B receptors in central neurons, consistent with their enrichment at glutamatergic synapses.</abstract><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>18579521</pmid><doi>10.1074/jbc.M802419200</doi></addata></record> |
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title | The Availability of Surface GABAB Receptors Is Independent of γ-Aminobutyric Acid but Controlled by Glutamate in Central Neurons |
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