Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

ATP Synthase: Structure01:18

ATP Synthase: Structure

13.0K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
13.0K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.9K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
5.9K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

15.1K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
15.1K
Structural Protein Function01:56

Structural Protein Function

2.8K
2.8K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.6K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.6K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

13.4K
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...
13.4K

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

Evaluation of DNA encoded library and machine learning model combinations for hit discovery.

npj drug discovery·2026
Same author

Probing the limits of genetic recoding using multi-omics-guided evolution.

Nature communications·2026
Same author

Correction: 요추 분리추간판의 영상 소견.

Journal of the Korean Society of Radiology·2026
Same author

Target-driven machine learning-enabled virtual screening (TAME-VS) enables prioritization of AKR1C3 inhibitors.

Communications chemistry·2026
Same author

Predictive value of primary tumour SUV<sub>max</sub> on <sup>18</sup>F-fluoro-2-deoxy-D-glucose positron emission tomography/computed tomography in patients undergoing fertility-sparing treatment for early endometrial cancer.

European journal of obstetrics, gynecology, and reproductive biology·2026
Same author

Structural dynamics of kappa opioid receptor interactions with β-arrestin 1.

Nature communications·2026

関連する実験動画

Updated: Sep 4, 2025

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
09:33

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

7.3K

SHOC2-MRAS-PP1Cホロフォスファタゼ複合体の構造機能分析

Jason J Kwon1,2,3, Behnoush Hajian4, Yuemin Bian4

  • 1Cancer Program, Broad Institute of MIT and Harvard, Cambridge, MA, USA.

Nature
|July 13, 2022
PubMed
まとめ

SHOC2-MRAS-PP1C複合体は細胞のシグナル伝達を制御する. 研究者はその構造を決定し,RASopathiesの変異がどのようにその活動を強化し,がん治療の開発の洞察を提供することを明らかにしました.

さらに関連する動画

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein
11:01

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein

Published on: March 31, 2010

18.3K
F&#246;rster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Published on: March 16, 2022

2.6K

関連する実験動画

Last Updated: Sep 4, 2025

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
09:33

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

7.3K
Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein
11:01

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein

Published on: March 31, 2010

18.3K
F&#246;rster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Published on: March 16, 2022

2.6K

科学分野:

  • 分子生物学
  • 構造生物学
  • 生物化学

背景:

  • ミトゲン活性化タンパク質キナーゼ (MAPK) カスケードを含む受容体チロシンキナーゼ (RTK) -RASシグナリングは,細胞増殖と生存を制御する.
  • SHOC2-MRAS-PP1Cホロフォスファテーゼ複合体は,RAFタンパク質を脱酸化することによってRTK-RASシグナル伝達に不可欠であり,それによってMAPKシグナル伝達を活性化します.
  • この複合体の細菌系機能増強変異はRASopathy症候群を引き起こすが,その構造と組み立ては不明である.

研究 の 目的:

  • SHOC2-MRAS-PP1Cホロフォスファターゼ複合体の構造と組成を解明する.
  • ホロ酵素の相互作用と複雑な組み立ての順序を規定する生体物理的原理を定義する.
  • 深層変異スキャニングを用いてSHOC2変異の機能的影響を調査する.

主な方法:

  • SHOC2- MRAS- PP1C複合体の高解像度構造を決定するために,冷凍電子顕微鏡 (冷凍EM) が使用された.
  • 多数のSHOC2ミセンス変異の機能的影響を評価するために,深層変異スキャンが行われました.
  • ホロ酵素の相互作用と組成を分析するために生体物理的手法を使用した.

主要な成果:

  • この研究では,SHOC2- MRAS- PP1C複合体の構造が解明され,SHOC2,MRAS,およびPP1Cの相互作用が詳細に示されました.
  • SHOC2はMRASとPP1Cと,レウシンに富んだリピート領域とN端の乱れた領域を通じて相互作用する.
  • 複合組成はSHOC2-PP1C結合で開始され,GTP負荷のMRASによって安定化され,RASopathy変異が活性化する方法を説明します.

結論:

  • この研究は,SHOC2-MRAS-PP1Cホロフォスファタゼ複合体の包括的な構造機能モデルを提供します.
  • この発見は,RAS病と癌に関連した変異が複合活性を増強する方法を明らかにしています.
  • 結合相互作用の詳細な理解は,標的治療法の開発を導くことができます.