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関連する概念動画

Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

17.1K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
6.3K
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

16.0K
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...
16.0K
Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

3.9K
Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.6K
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
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関連する実験動画

Updated: Dec 20, 2025

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

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ヒトER膜タンパク質複合体による膜挿入の構造的基礎

Tino Pleiner1, Giovani Pinton Tomaleri1, Kurt Januszyk1

  • 1Division of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Ave., Pasadena, CA 91125, USA.

Science (New York, N.Y.)
|May 23, 2020
PubMed
まとめ
この要約は機械生成です。

エンドプラズマ網膜タンパク質複合体 (EMC) は,遠水性タンパク質ヘリクスを細胞膜に挿入する. その構造は,この重要な生体生成のステップを容易にする,水性経路と脂質薄化のメカニズムを明らかにします.

さらに関連する動画

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
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Reconstitution of Msp1 Extraction Activity with Fully Purified Components

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

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関連する実験動画

Last Updated: Dec 20, 2025

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

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Reconstitution of Msp1 Extraction Activity with Fully Purified Components
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Reconstitution of Msp1 Extraction Activity with Fully Purified Components

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

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科学分野:

  • 生物化学
  • 分子生物学
  • 構造生物学

背景:

  • 膜タンパク質バイオゲネシスには,脂質二重層に水害性トランスメブランヘリクスの挿入が必要です.
  • エンドプラズマ網膜 (ER) 膜タンパク質複合体 (EMC) は,このプロセスに不可欠な保存インセルターゼである.
  • EMCの構造とメカニズムを理解することは タンパク質の挿入経路を解読するのに不可欠です

研究 の 目的:

  • 人間のEMCの高解像度構造を決定する
  • EMCが膜タンパク質の挿入を容易にする分子メカニズムを解明する.

主な方法:

  • 脂質ナノディスクのヒトEMCの冷凍電子顕微鏡 (冷凍EM)
  • 原子模型を作りました
  • 構造による突然変異

主要な成果:

  • ヒトのEMCのほぼ完全な原子モデルが 3.4アングストームの解像度で決定されました.
  • 基板の挿入はメチオニンに富んだ細胞循環に依存する.
  • 挿入は,EMC3とEMC6サブユニットによって形成された水性前庭を通して起こります.
  • EMCは局所的な膜薄化と陽性電荷パッチを使用して挿入エネルギーを低下させる.

結論:

  • EMCは,効率的なタンパク質挿入のために,水性前庭と膜調節を含むユニークな構造メカニズムを使用しています.
  • この研究は 膜タンパク質の生体形成の 基本的なステップに関する 原子レベルの洞察を提供します
  • この発見は,他の膜タンパク質挿入機構を理解するための枠組みを提供します.