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

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

12.1K
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...
12.1K
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

2.2K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.2K
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

15.5K
Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
15.5K
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

7.3K
Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
7.3K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

5.1K
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...
5.1K
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

7.3K
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
7.3K

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

B cell-intrinsic IRF8 transcriptionally reprograms antigen presentation to sustain CD8⁺ T cell antitumor immunity.

bioRxiv : the preprint server for biology·2026
Same author

Histone chaperone HIRA regulates adiponectin expression and obesity-associated adipose expansion by facilitating Pol II pause release.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Histone H3.3 ensures cell proliferation and genomic stability during myeloid cell development.

iScience·2026
Same author

Structure and mechanism of inhibition of lysine demethylase 2A (KDM2A) by compound 183c.

Communications chemistry·2026
Same author

Structural Transformation of a BRAF Inhibitor into a Selective PKR Inhibitor.

Journal of medicinal chemistry·2026
Same author

HIRA-mediated H3.3 deposition preserves hepatocyte cell identity during liver aging.

Research square·2026

関連する実験動画

Updated: Apr 26, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP
08:05

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

18.0K

PKR二分化,自己リン酸化,eIF2α基板認識のメカニズム的な関連性

Madhusudan Dey1, Chune Cao, Arvin C Dar

  • 1Laboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.

Cell
|September 24, 2005
PubMed
まとめ
この要約は機械生成です。

タンパク質キナーゼPKRは,

さらに関連する動画

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

7.8K
Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle
10:05

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

Published on: March 5, 2019

6.1K

関連する実験動画

Last Updated: Apr 26, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP
08:05

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

18.0K
Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

7.8K
Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle
10:05

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

Published on: March 5, 2019

6.1K

科学分野:

  • 分子生物学は分子生物学である.
  • ウイルス学 ウイルス学 ウイルス学
  • バイオケミストリー バイオケミストリー

背景:

  • タンパク質キナーゼPKRは,タンパク質合成を阻害する重要な抗ウイルスタンパク質です.
  • PKRの活性化は,二重鎖RNA結合によって誘発され,二分化と自己リン酸化につながります.
  • PKRによる翻訳開始因子eIF2alphaのリン酸化は,タンパク質合成を停止する.

研究 の 目的:

  • 規制ドメインとは独立してPKRを活性化する変異を特定する.
  • PKR活性化と基質認識におけるキナーゼ触媒ドメインの役割を明らかにする.
  • PKR活性化のメカニズムとそのeIF2alpha.と相互作用を定義する.

主な方法:

  • サイト・ディレクテッド・ミュータゲネシスで,PKRの変種を生成する.
  • 自動リン酸化とeIF2αリン酸化を測定するためのインビトロキナーゼアッセイ.
  • PKR触媒ドメイン内の変異と保存された残留物の分析.

主要な成果:

  • PKRを活性化する変異は,触媒ドメインの二分化表面にマッピングされた.
  • この表面の特定の変異は,PKR自己リン酸化とeIF2αリン酸化を阻害しました.
  • Thr446の変異はeIF2αリン酸化とウイルスの擬似基板結合を阻害する.
  • 触媒ドメイン内のヘリックス alphaGは,eIF2alpha認識に不可欠であると特定されました.

結論:

  • 触媒ドメインの二分化は,秩序あるPKR活性化における重要なステップです.
  • Thr446の自己リン酸化と特定のeIF2α基板結合は,下流イベントである.
  • この発見は,PKRの抗ウイルス活性に関する分子機構の洞察を提供します.