PRIP, a novel Ins(1,4,5)P3 binding protein, functional significance in Ca2+ signaling and extension to neuroscience and beyond

Takashi Kanematsu, Hiroshi Takeuchi, Miho Terunuma, Masato Hirata

研究成果: ジャーナルへの寄稿小調査

20 引用 (Scopus)

抄録

Investigation of chemically synthesized inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] analogs has led to the isolation of a novel binding protein with a molecular size of 130 kDa, characterized as a molecule with similar domain organization to phospholipase C-δ1 (PLC-δ1) but lacking the enzymatic activity. An isoform of the molecule was subsequently identified, and these molecules have been named PRIP (PLC-related, but catalytically inactive protein), with the two isoforms named PRIP-1 and -2. Regarding its ability to bind Ins(1,4,5)P3 via the pleckstrin homology domain, the involvement of PRIP-1 in Ins(1,4,5)P3-mediated Ca2+ signaling was examined using COS-1 cells overexpressing PRIP-1 and cultured neurons prepared from PRIP-1 knockout mice. Yeast two hybrid screening of a brain cDNA library using a unique N-terminus as bait identified GABARAP (GABAA receptor associated protein) and PP1 (protein phosphatase 1), which led us to examine the possible involvement of PRIP in GABAA receptor signaling. For this purpose PRIP knock-out mice were analyzed for GABAA receptor function in relation to the action of benzodiazepines from the electrophysiological and behavioral aspects. During the course of these experiments we found that PRIP also binds to the β-subunit of GABAA receptors and PP2A (protein phosphtase 2A). Here, we summarize how PRIP is involved in Ins(1,4,5)P3-mediated Ca2+ signaling and GABAA receptor signaling based on the characteristics of binding molecules.

元の言語英語
ページ(範囲)305-314
ページ数10
ジャーナルMolecules and Cells
20
発行部数3
出版物ステータス出版済み - 2005

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Neurosciences
Carrier Proteins
GABA-A Receptors
Proteins
Knockout Mice
Protein Isoforms
Protein Phosphatase 1
Inositol 1,4,5-Trisphosphate
COS Cells
Type C Phospholipases
Benzodiazepines
Gene Library
Yeasts
Neurons

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

これを引用

PRIP, a novel Ins(1,4,5)P3 binding protein, functional significance in Ca2+ signaling and extension to neuroscience and beyond. / Kanematsu, Takashi; Takeuchi, Hiroshi; Terunuma, Miho; Hirata, Masato.

:: Molecules and Cells, 巻 20, 番号 3, 2005, p. 305-314.

研究成果: ジャーナルへの寄稿小調査

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abstract = "Investigation of chemically synthesized inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] analogs has led to the isolation of a novel binding protein with a molecular size of 130 kDa, characterized as a molecule with similar domain organization to phospholipase C-δ1 (PLC-δ1) but lacking the enzymatic activity. An isoform of the molecule was subsequently identified, and these molecules have been named PRIP (PLC-related, but catalytically inactive protein), with the two isoforms named PRIP-1 and -2. Regarding its ability to bind Ins(1,4,5)P3 via the pleckstrin homology domain, the involvement of PRIP-1 in Ins(1,4,5)P3-mediated Ca2+ signaling was examined using COS-1 cells overexpressing PRIP-1 and cultured neurons prepared from PRIP-1 knockout mice. Yeast two hybrid screening of a brain cDNA library using a unique N-terminus as bait identified GABARAP (GABAA receptor associated protein) and PP1 (protein phosphatase 1), which led us to examine the possible involvement of PRIP in GABAA receptor signaling. For this purpose PRIP knock-out mice were analyzed for GABAA receptor function in relation to the action of benzodiazepines from the electrophysiological and behavioral aspects. During the course of these experiments we found that PRIP also binds to the β-subunit of GABAA receptors and PP2A (protein phosphtase 2A). Here, we summarize how PRIP is involved in Ins(1,4,5)P3-mediated Ca2+ signaling and GABAA receptor signaling based on the characteristics of binding molecules.",
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