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関連する概念動画

What are Second Messengers?01:12

What are Second Messengers?

Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...

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関連する実験動画

Updated: May 10, 2026

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation
10:52

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation

Published on: January 6, 2016

フォスファディチルイノシトール3リン酸塩を承認する.

S Misra1, G J Miller, J H Hurley

  • 1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Cell
|December 6, 2001
PubMed
まとめ
この要約は機械生成です。

フォスファチチドリノシトール3リン酸 (PI3P) は,FYVEとPXドメイン経由で内体タンパク質の局所化を誘導する. 新しい構造は,PI3Pの特定の化学相互作用がそれを他の脂質から区別する方法を明らかにします.

さらに関連する動画

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
07:26

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

関連する実験動画

Last Updated: May 10, 2026

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation
10:52

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation

Published on: January 6, 2016

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
07:26

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

科学分野:

  • バイオケミストリー バイオケミストリー
  • 細胞生物学 細胞生物学
  • 構造生物学 構造生物学とは

背景:

  • フォスファチチドリノシトール3酸塩 (PI3P) は,内体内密輸における重要なシグナル伝達脂質である.
  • FYVEとPXドメインはPI3Pと結合し,タンパク質の局所化を媒介することが知られている.
  • PI3P認識の分子基礎を理解することは,エンドソーマの分類機構の解読に不可欠です.

研究 の 目的:

  • FYVEとPXドメインによるPI3P認識の構造的基礎を明らかにする.
  • これらのドメインがPI3Pを他のフォスホイノシチドからどのように区別するかを理解するために.
  • 内体タンパク質の局所化を制御するPI3Pの役割についての洞察を提供するため.

主な方法:

  • X線結晶学を使用して,PI3Pと複合したFYVEおよびPXドメインの構造を決定しました.
  • 構造分析は,タンパク質ドメインとフォスホイノシチドヘッドグループ間の相互作用に焦点を当てました.
  • 他のフォスホイノシチドとの比較分析が行われました.

主要な成果:

  • 新しい構造は,FYVE/PXドメインとPI3Pヘッドグループ間の詳細な相互作用を明らかにします.
  • 特定の水素結合と,フォスファートとヒドロキシル基を含む静電相互作用が特定されました.
  • これらの相互作用は,PI3PをPI ((4,5) P2.2.などの他のフォスホイノシチドから正確に区別します.

結論:

  • 解明された構造は,PI3Pの特異性に対する分子的な説明を提供します.
  • これらの発見は,内体タンパク質標的化におけるPI3P結合ドメインの重要な役割を強調しています.
  • この研究は,内体機能の脂質媒介調節を理解するための枠組みを提供します.