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関連する概念動画

Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
ER Retrieval Pathway01:45

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

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関連する実験動画

Updated: Jul 6, 2026

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 8, 2013

VPS4 ATPasesによるESCRT-III認識について

Melissa D Stuchell-Brereton1, Jack J Skalicky, Collin Kieffer

  • 1Department of Biochemistry, Room 4100, 15 N. Medical Drive East, University of Utah, Salt Lake City, Utah 84112-5650, USA.

Nature
|October 12, 2007
PubMed
まとめ

研究者らは,VPS4 ATPasesがESCRT-IIIタンパク質 (CHMP) を認識し,HIVの芽生え,内分体分類,細胞分裂のための膜分裂を駆動することを発見しました. このメカニズムは,ウイルス,膀,子細胞の放出に不可欠です.

科学分野:

  • 細胞生物学 細胞生物学
  • 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

背景:

  • 輸送 (ESCRT) 経路に必要な内分体分類複合体は,HIVの芽生えと細胞運動などのプロセスにおける膜分裂に不可欠です.
  • VPS4 ATPasesは,ESCRT-III複合体を膜で分解するこの経路の鍵です.

研究 の 目的:

  • VPS4 ATPasesがESCRT-IIIタンパク質を認識し,相互作用する分子メカニズムを解明する.
  • この相互作用が膜分裂の出来事をどのように促進するかを理解する.

主な方法:

  • VPS4A MIT-CHMP1AおよびVPS4B MIT-CHMP2B複合体の構造分析について.
  • 結合相互作用を調査するためのサイト誘導性変異.
  • VPS4の徴募,エンドソームの分類,HIVの芽生えを評価する機能的検査.

主要な成果:

  • VPS4AとVPS4Bのマイクロチューブル相互作用および輸送 (MIT) ドメインは,CHMP1-3タンパク質に保存されたモチーフを結合します.
  • 構造的研究では,VPS4 MIT領域内のCHMPモチーフのユニークな結合モードが明らかになりました.
  • この相互作用を妨げる突然変異は,複数の細胞プロセスにおけるVPS4の機能を損なう.

さらに関連する動画

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays
12:25

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

Published on: September 28, 2018

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

関連する実験動画

Last Updated: Jul 6, 2026

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 8, 2013

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays
12:25

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

Published on: September 28, 2018

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

結論:

  • VPS4 ATPasesは,MITドメイン内の特定の相互作用を通じてCHMP基板を認識します.
  • この認識メカニズムは,ウイルスの放出,エンドソーマの密輸,細胞分裂における膜分裂を媒介するために不可欠です.