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関連する概念動画

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.2K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.2K
Energy to Drive Translocation01:37

Energy to Drive Translocation

2.1K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
2.1K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.6K
2.6K
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

7.0K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
7.0K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

4.1K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
4.1K
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

5.3K
Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
5.3K

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関連する実験動画

Updated: Sep 10, 2025

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
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Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Published on: March 1, 2022

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AIによる移行経路サンプリングによって捕捉されたSTIM1のトランスメブランヘリックス二分化

Ferdinand Horvath1, Hendrik Jung2, Herwig Grabmayr3

  • 1Institute of Theoretical Physics, Johannes Kepler University Linz, 4040 Linz, Austria.

Proceedings of the National Academy of Sciences of the United States of America
|August 26, 2025
PubMed
まとめ

ストロマル相互作用分子1 (STIM1) のタンパク質二酸化は,カルシウム検出の鍵です. AIによるシミュレーションでは,3つの異なるSTIM1トランスメブランヘリックスダイマー構成が明らかになり,そのメカニズムが明確になりました.

キーワード:
STIM1 についてTM・ヘリックス・ディメリゼーション貯蔵されたカルシウム入力移行経路のサンプリング

さらに関連する動画

Chemical Dimerization-Induced Protein Condensates on Telomeres
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Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

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関連する実験動画

Last Updated: Sep 10, 2025

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
09:17

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Published on: March 1, 2022

3.2K
Chemical Dimerization-Induced Protein Condensates on Telomeres
08:52

Chemical Dimerization-Induced Protein Condensates on Telomeres

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.3K

科学分野:

  • バイオ物理学
  • 分子生物学
  • カルシウムシグナル

背景:

  • ストロマル相互作用分子1 (STIM1) は,エンドプラズマ網膜 (ER) に位置する重要なCa2+センサーである.
  • ER Ca2+の減少はSTIM1の構造変化を引き起こし,カルシウムシグナル伝達経路を開始する.
  • STIM1のトランスメブラン (TM) ドメインの二極化はこのプロセスの重要な初期段階です.

研究 の 目的:

  • STIM1 経膜ヘリクスの二分化を制御する原子学的メカニズムを解明する.
  • 異なるSTIM1ダイマー構成とその関連移行状態を特定する.
  • 実験的な変異性研究でシミュレーション結果を検証する.

主な方法:

  • 広範な分子ダイナミクス (MD) シミュレーションのために,AIによる移行経路サンプリング (aimmd) を利用した.
  • ERを模倣した脂質二層環境で全原子MDシミュレーションを行った.
  • インビトロ光ベースの二分化傾向実験と統合された計算結果.

主要な成果:

  • 以前の実験の不一致を解決した3つの異なる,共存するSTIM1 TMヘリックスダイマー構成を特定しました.
  • 主要なダイマー構成は,SxxxGモチーフによって安定したX形インターフェースを特徴としています.
  • SxxxGモチーフの変異は,実験試験でSTIM1二分化傾向を変化させた.
  • トランジション・ステート・アンサンブルを特徴付け,光間ヘリカルコンタクトの重要性を強調した.

結論:

  • AIによるMDシミュレーションは STIM1の二分化のような希少な分子現象に 前例のない原子学的詳細を提供します.
  • STIM1 TMヘリックス二重化は,光相互作用によって影響される複数の経路で発生します.
  • これらの発見は,細胞のカルシウムホメオスタシスにおけるSTIM1の役割のメカニズム的理解を提供します.