Identification of postsynaptic phosphatidylinositol-4,5-bisphosphate (PIP2) roles for synaptic plasticity using chemically induced dimerization

Abstract Phosphatidylinositol-4,5-bisphosphate (PIP2), one of the key phospholipids, directly interacts with several membrane and cytosolic proteins at neuronal plasma membranes, leading to changes in neuronal properties including the feature and surface expression of ionotropic receptors. Although...

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Autores principales:	Su-Jeong Kim, Min-Jae Jeong, Hee-Jung Jo, Jung Hoon Jung, Bong-Kiun Kaang, Yun-Beom Choi, Joung-Hun Kim
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7f86a53965e24cea9156e3febe658d11
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spelling	oai:doaj.org-article:7f86a53965e24cea9156e3febe658d112021-12-02T16:08:22ZIdentification of postsynaptic phosphatidylinositol-4,5-bisphosphate (PIP2) roles for synaptic plasticity using chemically induced dimerization10.1038/s41598-017-03520-32045-2322https://doaj.org/article/7f86a53965e24cea9156e3febe658d112017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03520-3https://doaj.org/toc/2045-2322Abstract Phosphatidylinositol-4,5-bisphosphate (PIP2), one of the key phospholipids, directly interacts with several membrane and cytosolic proteins at neuronal plasma membranes, leading to changes in neuronal properties including the feature and surface expression of ionotropic receptors. Although PIP2 is also concentrated at the dendritic spines, little is known about the direct physiological functions of PIP2 at postsynaptic as opposed to presynaptic sites. Most previous studies used genetic and pharmacological methods to modulate enzymes that alter PIP2 levels, making it difficult to delineate time- or region-specific roles of PIP2. We used chemically-induced dimerization to translocate inositol polyphosphate 5-phosphatase (Inp54p) to plasma membranes in the presence of rapamycin. Upon redistribution of Inp54p, long-term depression (LTD) induced by low-frequency stimulation was blocked in the mouse hippocampal CA3-CA1 pathway, but the catalytically-dead mutant did not affect LTD induction. Collectively, PIP2 is critically required for induction of LTD whereas translocation of Inp54p to plasma membranes has no effect on the intrinsic properties of the neurons, basal synaptic transmission, long-term potentiation or expression of LTD.Su-Jeong KimMin-Jae JeongHee-Jung JoJung Hoon JungBong-Kiun KaangYun-Beom ChoiJoung-Hun KimNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Su-Jeong Kim Min-Jae Jeong Hee-Jung Jo Jung Hoon Jung Bong-Kiun Kaang Yun-Beom Choi Joung-Hun Kim Identification of postsynaptic phosphatidylinositol-4,5-bisphosphate (PIP2) roles for synaptic plasticity using chemically induced dimerization
description	Abstract Phosphatidylinositol-4,5-bisphosphate (PIP2), one of the key phospholipids, directly interacts with several membrane and cytosolic proteins at neuronal plasma membranes, leading to changes in neuronal properties including the feature and surface expression of ionotropic receptors. Although PIP2 is also concentrated at the dendritic spines, little is known about the direct physiological functions of PIP2 at postsynaptic as opposed to presynaptic sites. Most previous studies used genetic and pharmacological methods to modulate enzymes that alter PIP2 levels, making it difficult to delineate time- or region-specific roles of PIP2. We used chemically-induced dimerization to translocate inositol polyphosphate 5-phosphatase (Inp54p) to plasma membranes in the presence of rapamycin. Upon redistribution of Inp54p, long-term depression (LTD) induced by low-frequency stimulation was blocked in the mouse hippocampal CA3-CA1 pathway, but the catalytically-dead mutant did not affect LTD induction. Collectively, PIP2 is critically required for induction of LTD whereas translocation of Inp54p to plasma membranes has no effect on the intrinsic properties of the neurons, basal synaptic transmission, long-term potentiation or expression of LTD.
format	article
author	Su-Jeong Kim Min-Jae Jeong Hee-Jung Jo Jung Hoon Jung Bong-Kiun Kaang Yun-Beom Choi Joung-Hun Kim
author_facet	Su-Jeong Kim Min-Jae Jeong Hee-Jung Jo Jung Hoon Jung Bong-Kiun Kaang Yun-Beom Choi Joung-Hun Kim
author_sort	Su-Jeong Kim
title	Identification of postsynaptic phosphatidylinositol-4,5-bisphosphate (PIP2) roles for synaptic plasticity using chemically induced dimerization
title_short	Identification of postsynaptic phosphatidylinositol-4,5-bisphosphate (PIP2) roles for synaptic plasticity using chemically induced dimerization
title_full	Identification of postsynaptic phosphatidylinositol-4,5-bisphosphate (PIP2) roles for synaptic plasticity using chemically induced dimerization
title_fullStr	Identification of postsynaptic phosphatidylinositol-4,5-bisphosphate (PIP2) roles for synaptic plasticity using chemically induced dimerization
title_full_unstemmed	Identification of postsynaptic phosphatidylinositol-4,5-bisphosphate (PIP2) roles for synaptic plasticity using chemically induced dimerization
title_sort	identification of postsynaptic phosphatidylinositol-4,5-bisphosphate (pip2) roles for synaptic plasticity using chemically induced dimerization
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/7f86a53965e24cea9156e3febe658d11
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_version_	1718384540041347072

Identification of postsynaptic phosphatidylinositol-4,5-bisphosphate (PIP2) roles for synaptic plasticity using chemically induced dimerization

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