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関連する概念動画

Phosphorylation01:02

Phosphorylation

51.2K
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...
51.2K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

13.5K
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...
13.5K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

4.0K
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...
4.0K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

8.9K
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...
8.9K
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

7.3K
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...
7.3K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.3K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
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関連する実験動画

Updated: Sep 15, 2025

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

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ダイナミックな細胞プロセスを調節する酸化誘導分子

Rajaiah Pergu1, Vedagopuram Sreekanth1,2,3, Praveen Kokkonda1

  • 1Chemical Biology and Therapeutics Science, Broad Institute of MIT and Harvard, Cambridge, Massachusetts 02142, United States.

Journal of the American Chemical Society
|July 14, 2025
PubMed
まとめ
この要約は機械生成です。

リン酸化誘導キメリック小分子 (PHICS) を使用した新しいプラットフォームは,制御されたタンパク質リン酸化を可能にします. この進歩により 癌の信号伝達や ニューロンの機能といった 細胞のプロセスを 厳格に制御できます

さらに関連する動画

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

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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

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関連する実験動画

Last Updated: Sep 15, 2025

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

8.5K
Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

8.3K
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

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科学分野:

  • 分子生物学
  • セルラー・シグナル
  • 生物化学

背景:

  • タンパク質のリン酸化は 細胞のコミュニケーションに不可欠です
  • 既存のリン酸化誘発キメリック小分子 (PHICS) は,血清飢餓と標的過剰表現への依存を含む制限があります.
  • 以前のPHICSでは,AMP活性化タンパク質キナーゼ (AMPK) の募集と活性に対する制御が限られていた.

研究 の 目的:

  • 生理学的条件下で制御されたタンパク質のリン酸化のための新しいAMPK PHICSプラットフォームを開発する.
  • これまでのPHICS技術の限界を克服するために
  • 細胞の重要なプロセスを制御する プラットフォームの有用性を示すために

主な方法:

  • 先進的なAMPK PHICSプラットフォームの開発
  • 腫瘍性シグナル伝達経路を制御するためにPHICSの適用
  • 神経細胞のタンパク質相分離を調節するためにPHICSを使用します.

主要な成果:

  • 新しいAMPK PHICSプラットフォームは,血清の飢餓なしで効果的に動作します.
  • 標的タンパク質の量および時間制御されたリン酸化を可能にします.
  • PHICSはがん細胞における腫瘍性ブルトンチロシンキナーゼ (BTK) を成功裏に抑制し,神経細胞におけるリプリンα3相分離を制御した.

結論:

  • 開発されたAMPK PHICSプラットフォームは,タンパク質のリン酸化を正確に制御します.
  • この技術は 癌や神経科学を含む 様々な細胞プロセスに適用できます
  • このプラットフォームは,基礎研究と生物医学アプリケーションの大きな可能性を秘めています.