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Identification of postsynaptic phosphatidylinositol-4,5-bisphosphate (PIP2) roles for synaptic plasticity using chemically induced dimerization.
Kim, Su-Jeong; Jeong, Min-Jae; Jo, Hee-Jung; Jung, Jung Hoon; Kaang, Bong-Kiun; Choi, Yun-Beom; Kim, Joung-Hun.
Afiliación
  • Kim SJ; Department of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Gyungbuk, 37673, Korea.
  • Jeong MJ; Department of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Gyungbuk, 37673, Korea.
  • Jo HJ; Department of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Gyungbuk, 37673, Korea.
  • Jung JH; Department of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Gyungbuk, 37673, Korea.
  • Kaang BK; Department of Biological Sciences, College of Natural Sciences, Seoul National University, Seoul, 08826, Korea.
  • Choi YB; Neurology Service, VA New Jersey Health Care System, East Orange, New Jersey, 07018, USA.
  • Kim JH; Department of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, Gyungbuk, 37673, Korea. joungkim@postech.ac.kr.
Sci Rep ; 7(1): 3351, 2017 06 13.
Article en En | MEDLINE | ID: mdl-28611378
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.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sinapsis / Potenciación a Largo Plazo / Fosfatidilinositol 4,5-Difosfato / Neuronas Tipo de estudio: Diagnostic_studies Límite: Animals / Humans Idioma: En Revista: Sci Rep Año: 2017 Tipo del documento: Article Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sinapsis / Potenciación a Largo Plazo / Fosfatidilinositol 4,5-Difosfato / Neuronas Tipo de estudio: Diagnostic_studies Límite: Animals / Humans Idioma: En Revista: Sci Rep Año: 2017 Tipo del documento: Article Pais de publicación: Reino Unido