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関連する概念動画

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.6K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
13.2K
Rab Proteins01:14

Rab Proteins

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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...
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

3.6K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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Updated: Sep 10, 2025

Avidity-based Extracellular Interaction Screening AVEXIS for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
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Eps15とパートナータンパク質Dab2の乱交的で多価な相互作用は,複雑な相互作用ネットワークを生成する.

Andromachi Papagiannoula1,2, Ida Marie Vedel1, Kathrin Motzny1

  • 1Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, Berlin, Germany.

Nature communications
|August 21, 2025
PubMed
まとめ

Eps15 EHドメインは,固有の無秩序領域 (IDR) を含むタンパク質モチーフに乱交的に結合する. この相互作用ネットワークは,早期のクラトリン媒介性内細胞化とDab2をEps15凝縮物へと誘導する.

さらに関連する動画

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP
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関連する実験動画

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Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
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科学分野:

  • 細胞生物学
  • 分子生物学
  • 生物化学

背景:

  • クラトリン媒介性内細胞分裂 (CME) は細胞プロセスにとって極めて重要です.
  • Eps15タンパク質の相互作用は,CMEにとって重要なものです.
  • Eps15 EHドメインは,本質的に乱れた領域 (IDR) でAsn-Pro-Phe (NPF) モチーフを結合する.

研究 の 目的:

  • Eps15 EHドメインと乱れたDab2断片の相互作用を調査する.
  • 初期のCMEにおけるタンパク質の相互作用を制御する分子メカニズムを解明する.
  • Eps15媒介性エンドサイトーシスにおける結合乱交の役割を理解する.

主な方法:

  • 核磁共振 (NMR) スペクトロスコーピー
  • タンパク質とタンパク質の相互作用を研究する生化学的測定法
  • 本質的に無秩序な地域 (IDR) とその拘束力のあるパートナーの分析

主要な成果:

  • Eps15 EHドメインは,NPFおよび他のフェニララニンを含むモチーフを認識する結合乱交性を示す.
  • Eps15自身のIDR (Eps15_IDR) はEHドメインと相互作用し,自己抑制メカニズムを示唆しています.
  • Eps15_IDRとDab2の断片は同時にEH123に結合し,ダイナミックなネットワークを形成し,凝縮物形成を促進する.

結論:

  • Eps15 EHドメインの結合性はそのCMEにおける機能の鍵である.
  • 競争と協力の相互作用がDab2の徴集とコンデンサットの組立を規制する.
  • これらの発見は,内細胞タンパク質ネットワークのダイナミックな調節に関する分子洞察を提供します.