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α/β-Hydrolase domain-containing 6 (ABHD6) negatively regulates the surface delivery and synaptic function of AMPA receptors.

In the brain, AMPA-type glutamate receptors are major postsynaptic receptors at excitatory synapses that mediate fast neurotransmission and synaptic plasticity. α/β-Hydrolase domain-containing 6 (ABHD6), a monoacylglycerol lipase, was previously found to be a component of AMPA receptor macromolecula... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America May 10, 2016, Vol.113(19), pp.E2695-E2704
Main Author: Wei, Mengping
Other Authors: Zhang, Jian , Jia, Moye , Yang, Chaojuan , Pan, Yunlong , Li, Shuaiqi , Luo, Yiwen , Zheng, Junyuan , Ji, Jianguo , Chen, Jianguo , Hu, Xinli , Xiong, Jingwei , Shi, Yun , Zhang, Chen
Format: Electronic Article Electronic Article
Language: English
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ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1524589113
Link: http://search.proquest.com/docview/1788538263/?pq-origsite=primo
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title: α/β-Hydrolase domain-containing 6 (ABHD6) negatively regulates the surface delivery and synaptic function of AMPA receptors.
format: Article
creator:
  • Wei, Mengping
  • Zhang, Jian
  • Jia, Moye
  • Yang, Chaojuan
  • Pan, Yunlong
  • Li, Shuaiqi
  • Luo, Yiwen
  • Zheng, Junyuan
  • Ji, Jianguo
  • Chen, Jianguo
  • Hu, Xinli
  • Xiong, Jingwei
  • Shi, Yun
  • Zhang, Chen
subjects:
  • Action Potentials–Physiology
  • Animals–Metabolism
  • Cell Membrane–Cytology
  • Cells, Cultured–Physiology
  • Hek293 Cells–Metabolism
  • Hippocampus–Physiology
  • Humans–Physiology
  • Mice–Metabolism
  • Monoacylglycerol Lipases–Physiology
  • Neurons–Physiology
  • Protein Domains–Physiology
  • Receptors, Ampa–Physiology
  • Synaptic Transmission–Physiology
  • Receptors, Ampa
  • Abhd6 Protein, Mouse
  • Monoacylglycerol Lipases
  • Abhd6
  • Ampa Receptor
  • Receptor Trafficking
  • Synapses
ispartof: Proceedings of the National Academy of Sciences of the United States of America, May 10, 2016, Vol.113(19), pp.E2695-E2704
description: In the brain, AMPA-type glutamate receptors are major postsynaptic receptors at excitatory synapses that mediate fast neurotransmission and synaptic plasticity. α/β-Hydrolase domain-containing 6 (ABHD6), a monoacylglycerol lipase, was previously found to be a component of AMPA receptor macromolecular complexes, but its physiological significance in the function of AMPA receptors (AMPARs) has remained unclear. The present study shows that overexpression of ABHD6 in neurons drastically reduced excitatory neurotransmission mediated by AMPA but not by NMDA receptors at excitatory synapses. Inactivation of ABHD6 expression in neurons by either CRISPR/Cas9 or shRNA knockdown methods significantly increased excitatory neurotransmission at excitatory synapses. Interestingly, overexpression of ABHD6 reduced glutamate-induced currents and the surface expression of GluA1 in HEK293T cells expressing GluA1 and stargazin, suggesting a direct functional interaction between these two proteins. The C-terminal tail of GluA1 was required for the binding between of ABHD6 and GluA1. Mutagenesis analysis revealed a GFCLIPQ sequence in the GluA1 C terminus that was essential for the inhibitory effect of ABHD6. The hydrolase activity of ABHD6 was not required for the effects of ABHD6 on AMPAR function in either neurons or transfected HEK293T cells. Thus, these findings reveal a novel and unexpected mechanism governing AMPAR trafficking at synapses through ABHD6.
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1524589113
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleα/β-Hydrolase domain-containing 6 (ABHD6) negatively regulates the surface delivery and synaptic function of AMPA receptors.
creatorWei, Mengping ; Zhang, Jian ; Jia, Moye ; Yang, Chaojuan ; Pan, Yunlong ; Li, Shuaiqi ; Luo, Yiwen ; Zheng, Junyuan ; Ji, Jianguo ; Chen, Jianguo ; Hu, Xinli ; Xiong, Jingwei ; Shi, Yun ; Zhang, Chen
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identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1524589113
subjectAction Potentials–Physiology ; Animals–Metabolism ; Cell Membrane–Cytology ; Cells, Cultured–Physiology ; Hek293 Cells–Metabolism ; Hippocampus–Physiology ; Humans–Physiology ; Mice–Metabolism ; Monoacylglycerol Lipases–Physiology ; Neurons–Physiology ; Protein Domains–Physiology ; Receptors, Ampa–Physiology ; Synaptic Transmission–Physiology ; Receptors, Ampa ; Abhd6 Protein, Mouse ; Monoacylglycerol Lipases ; Abhd6 ; Ampa Receptor ; Receptor Trafficking ; Synapses
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descriptionIn the brain, AMPA-type glutamate receptors are major postsynaptic receptors at excitatory synapses that mediate fast neurotransmission and synaptic plasticity. α/β-Hydrolase domain-containing 6 (ABHD6), a monoacylglycerol lipase, was previously found to be a component of AMPA receptor macromolecular complexes, but its physiological significance in the function of AMPA receptors (AMPARs) has remained unclear. The present study shows that overexpression of ABHD6 in neurons drastically reduced excitatory neurotransmission mediated by AMPA but not by NMDA receptors at excitatory synapses. Inactivation of ABHD6 expression in neurons by either CRISPR/Cas9 or shRNA knockdown methods significantly increased excitatory neurotransmission at excitatory synapses. Interestingly, overexpression of ABHD6 reduced glutamate-induced currents and the surface expression of GluA1 in HEK293T cells expressing GluA1 and stargazin, suggesting a direct functional interaction between these two proteins. The C-terminal tail of GluA1 was required for the binding between of ABHD6 and GluA1. Mutagenesis analysis revealed a GFCLIPQ sequence in the GluA1 C terminus that was essential for the inhibitory effect of ABHD6. The hydrolase activity of ABHD6 was not required for the effects of ABHD6 on AMPAR function in either neurons or transfected HEK293T cells. Thus, these findings reveal a novel and unexpected mechanism governing AMPAR trafficking at synapses through ABHD6.
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titleα/β-Hydrolase domain-containing 6 (ABHD6) negatively regulates the surface delivery and synaptic function of AMPA receptors.
authorWei, Mengping ; Zhang, Jian ; Jia, Moye ; Yang, Chaojuan ; Pan, Yunlong ; Li, Shuaiqi ; Luo, Yiwen ; Zheng, Junyuan ; Ji, Jianguo ; Chen, Jianguo ; Hu, Xinli ; Xiong, Jingwei ; Shi, Yun ; Zhang, Chen
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