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関連する概念動画

The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

4.8K
The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
4.8K
Mitochondrial Membranes01:45

Mitochondrial Membranes

17.4K
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
17.4K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

5.0K
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...
5.0K
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

4.9K
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
4.9K
Contact-dependent Signaling01:19

Contact-dependent Signaling

47.7K
Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
Gap Junctions
In animal cells, gap junctions are formed...
47.7K
Animal Mitochondrial Genetics02:59

Animal Mitochondrial Genetics

9.3K
Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
9.3K

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関連する実験動画

Updated: Feb 16, 2026

Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
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Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights

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BRD4媒介のER膜接触により,機能的に異なるミトコンドリア亜型が生成されます.

Brandon Chen1, Drew C Stark2, Pankaj V Jadhav3

  • 1Cellular and Molecular Biology Program, University of Michigan Medical School, Ann Arbor, MI 48109, USA; Department of Molecular & Integrative Physiology, University of Michigan, Ann Arbor, MI 48109, USA.

Molecular cell
|February 14, 2026
PubMed
まとめ

研究者らは,BRD4.4を阻害することによって,エンドプラズマ網膜とミトコンドリア接触部位 (ERMCSs) を迅速に制御する薬であるフェドラチニブを発見した. この発見は,細胞代謝に影響を与える新しい表遺伝子経路を明らかにしています.

キーワード:
ブロモドメインタンパク質は,エンドプラズマ網膜-ミトコンドリアの接触部位高通量スクリーニングミトコンドリアの電子輸送鎖は

さらに関連する動画

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
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Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

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Simultaneous Measurement of Mitochondrial Calcium and Mitochondrial Membrane Potential in Live Cells by Fluorescent Microscopy
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Simultaneous Measurement of Mitochondrial Calcium and Mitochondrial Membrane Potential in Live Cells by Fluorescent Microscopy

Published on: January 24, 2017

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関連する実験動画

Last Updated: Feb 16, 2026

Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
07:55

Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights

Published on: June 16, 2023

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Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

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Simultaneous Measurement of Mitochondrial Calcium and Mitochondrial Membrane Potential in Live Cells by Fluorescent Microscopy
08:43

Simultaneous Measurement of Mitochondrial Calcium and Mitochondrial Membrane Potential in Live Cells by Fluorescent Microscopy

Published on: January 24, 2017

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科学分野:

  • 細胞生物学 細胞生物学
  • エピジェネティクス エピジェネティクス
  • メタボリック・レギュレーション

背景:

  • 臓器細胞間のコミュニケーションは,細胞の代謝に不可欠です.
  • エンドプラズマ網膜とミトコンドリアの接触部位 (ERMCS) は,相互作用の重要な部位である.
  • 現在のツールでは,ERMCSの規制を研究するための時間的なコントロールが欠如しています.

研究 の 目的:

  • ERMCSの時間制御のための新しいツールを特定する.
  • ERMCSの調節のメカニズムと代謝の役割を解明する.
  • ERMCSと代謝を結びつける新しいシグナル伝達経路を発見する.

主な方法:

  • 薬物スクリーニングは,ERMCSの豊富性の調節剤を特定するために行われます.
  • BRD4.4を標的とするFDAが承認した薬であるフェドラチニブを使用した.
  • ミトコンドリアとERの形態学,代謝性ホメオスタシス,電子輸送鎖の機能に対する評価された影響.

主要な成果:

  • フェドラチニブは,BRD4.4を阻害することにより,ERMCSの豊富性を劇的に増加させます.
  • フェドラチニブは,臓器形態と代謝的恒常性を迅速かつ可逆的に調節する.
  • ERMCSの調節は,ミトコンドリアの電子輸送連鎖複合体IIIに依存しています.

結論:

  • フェドラチニブは,ERMCSsの時間的な制御のためのツールを提供します.
  • BRD4を含む新しい表遺伝子経路は,ERMCSsを調節する.
  • この経路は,ERMCSを細胞代謝と結びつけ,新たな治療標的を提供している.