Structural basis of GABARAP-mediated GABAA receptor trafficking and functions on GABAergic synaptic transmission

Structural basis of GABARAP-mediated GABAA receptor trafficking and functions on GABAergic synaptic transmission

The GABARAP protein is known to support the stability of GABAA receptors (GABAARs) in synapses, but the underlying molecular mechanisms remained to be elucidated. Here authors use biochemistry, X-ray crystallography and electrophsyiology and show that GABARAP directly binds to a previously unappreci...

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Auteurs principaux: Jin Ye, Guichang Zou, Ruichi Zhu, Chao Kong, Chenjian Miao, Mingjie Zhang, Jianchao Li, Wei Xiong, Chao Wang
Format: article
Langue:EN
Publié: Nature Portfolio 2021
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Accès en ligne:https://doaj.org/article/7601d2b73eeb4f368fd223c36dd2f3fb
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spelling oai:doaj.org-article:7601d2b73eeb4f368fd223c36dd2f3fb2021-12-02T15:22:48ZStructural basis of GABARAP-mediated GABAA receptor trafficking and functions on GABAergic synaptic transmission10.1038/s41467-020-20624-z2041-1723https://doaj.org/article/7601d2b73eeb4f368fd223c36dd2f3fb2021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20624-zhttps://doaj.org/toc/2041-1723The GABARAP protein is known to support the stability of GABAA receptors (GABAARs) in synapses, but the underlying molecular mechanisms remained to be elucidated. Here authors use biochemistry, X-ray crystallography and electrophsyiology and show that GABARAP directly binds to a previously unappreciated region in the γ2 subunit of GABAAR.Jin YeGuichang ZouRuichi ZhuChao KongChenjian MiaoMingjie ZhangJianchao LiWei XiongChao WangNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Jin Ye
Guichang Zou
Ruichi Zhu
Chao Kong
Chenjian Miao
Mingjie Zhang
Jianchao Li
Wei Xiong
Chao Wang
Structural basis of GABARAP-mediated GABAA receptor trafficking and functions on GABAergic synaptic transmission
description The GABARAP protein is known to support the stability of GABAA receptors (GABAARs) in synapses, but the underlying molecular mechanisms remained to be elucidated. Here authors use biochemistry, X-ray crystallography and electrophsyiology and show that GABARAP directly binds to a previously unappreciated region in the γ2 subunit of GABAAR.
format article
author Jin Ye
Guichang Zou
Ruichi Zhu
Chao Kong
Chenjian Miao
Mingjie Zhang
Jianchao Li
Wei Xiong
Chao Wang
author_facet Jin Ye
Guichang Zou
Ruichi Zhu
Chao Kong
Chenjian Miao
Mingjie Zhang
Jianchao Li
Wei Xiong
Chao Wang
author_sort Jin Ye
title Structural basis of GABARAP-mediated GABAA receptor trafficking and functions on GABAergic synaptic transmission
title_short Structural basis of GABARAP-mediated GABAA receptor trafficking and functions on GABAergic synaptic transmission
title_full Structural basis of GABARAP-mediated GABAA receptor trafficking and functions on GABAergic synaptic transmission
title_fullStr Structural basis of GABARAP-mediated GABAA receptor trafficking and functions on GABAergic synaptic transmission
title_full_unstemmed Structural basis of GABARAP-mediated GABAA receptor trafficking and functions on GABAergic synaptic transmission
title_sort structural basis of gabarap-mediated gabaa receptor trafficking and functions on gabaergic synaptic transmission
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/7601d2b73eeb4f368fd223c36dd2f3fb
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