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関連する概念動画

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...
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...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

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関連する実験動画

Updated: Jun 4, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

セリン/スレオニンファスファタゼ:構造を通してのメカニズム

Yigong Shi1

  • 1Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China. shi-lab@tsinghua.edu.cn

Cell
|November 3, 2009
PubMed
まとめ

タンパク質フォスファタゼは,細胞シグナル伝達に不可欠です. このレビューでは,主要なタンパク質セリン/スレオニンフォスファタゼクラスのメカニズムを調査し,タンパク質フォスファタゼ2A (PP2A) の調節と機能に焦点を当てています.

科学分野:

  • バイオケミストリー バイオケミストリー
  • 分子生物学は分子生物学である.
  • 構造生物学 構造生物学とは

背景:

  • タンパク質のリン酸化は,細胞プロセスにおける重要な規制メカニズムである.
  • タンパク質セリン/スレオニンフォスファタゼ (PSP) は,リン酸基を除去することでキナーゼの活性に対抗する.
  • 限られた数のPSPは,多数の基板を脱リン化し,特定の規制メカニズムを必要とします.

研究 の 目的:

  • タンパク質セリン/スレオニンフォスファタゼ (PSP) 機能の生化学的および構造的基礎をレビューする.
  • 主要なPSPクラスにおける基板特異性および調節のメカニズムを解明する.
  • PSPにおけるタンパク質フォスファタゼ2A (PP2A) の重要性を強調する.

主な方法:

  • 酵素の活性と相互作用を研究するための生化学的測定法.
  • タンパク質の構造を決定するための構造生物学技術 (例えば,X線結晶学,冷凍EM)
  • 異なるフォスファタゼのクラスを比較するためのバイオ情報分析.

主要な成果:

  • PSPは,触媒および規制サブユニット相互作用 (例えば,PP1,PP2A) または固有のドメイン (例えば,PP2C,FCP/SCP) を含む多様な戦略を通じて特異性を達成します.

さらに関連する動画

Recombinant &#945;- &#946;- and &#947;-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
09:36

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

関連する実験動画

Last Updated: Jun 4, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Recombinant &#945;- &#946;- and &#947;-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
09:36

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

  • 詳細な構造的および生化学的データは,フォスファターゼ調節に関するメカニズム的洞察を提供します.
  • PP2Aは,特異性のために規制サブユニットに依存する主要なPSPクラスの例です.

    • 結論:

    • PSPメカニズムを理解することは,セルラー信号ネットワークを理解するために不可欠です.
    • PSPクラスによって採用されている異なる戦略は,デフォスフォリレーションの複雑さを強調しています.
    • PSP,特にPP2Aに関するさらなる研究は,治療的介入の可能性を秘めています.