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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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,...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...
Cadherins in Tissue Organization01:19

Cadherins in Tissue Organization

The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
Cell Sorting During Development
Cell sorting plays an...
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...

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Updated: May 7, 2026

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
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タイプIIカデリンエクトドメイン構造:古典的なカデリン特異性への影響

Saurabh D Patel1, Carlo Ciatto, Chien Peter Chen

  • 1Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.

Cell
|March 28, 2006
PubMed
まとめ

クラシックなカデリン (タイプIとII) は細胞結合を媒介する. 構造分析は,交換されたベータ鎖と保存されたトリプトファンの残留物によって駆動され,細胞特異性を決定する,タイプIIカデリンにおけるユニークな粘着性インターフェースを明らかにします.

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Last Updated: May 7, 2026

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科学分野:

  • 細胞生物学 細胞生物学
  • 構造生物学 構造生物学とは
  • バイオケミストリー バイオケミストリー

背景:

  • 古典的なカデリン (タイプIとII) は,重要な細胞粘着分子である.
  • 細胞外ドメインは,細胞間の認識と特異性を決定する.

研究 の 目的:

  • タイプIIの古典的なカデリンの細胞粘着特異性の構造的基礎を解明する.
  • タイプIとタイプIIのカデリンの接着剤インターフェイスを比較するために.

主な方法:

  • 3つのタイプIIカデリンからエクトドメイン領域の結晶構造の決定.
  • タンパク質のインターフェースと保存された残留物の分析.
  • キメリックカデリンを用いたインビトロおよびインビボ機能性アッセイ.

主要な成果:

  • II型カデリンは,細胞外カデリン-1 (EC1) ドメインの交換されたN端ベータ鎖を介して,粘着ジマーを形成する.
  • これらのインターフェースには,2つの保存されたトリプトファン残留物と,タイプIカデリンとは異なるユニークな水害性領域が特徴です.
  • タイプIとタイプIIのカデリンの両方のEC1ドメインは,細胞の粘着特異性をin vitroで決定する.
  • 化学カデリンの実験では,EC1ドメインの同一性が,体内におけるモーターニューロン分離におけるタイプIIカデリンの機能に決定的であることを示しています.

結論:

  • EC1ドメイン,特に構造的に定義された粘着性インターフェースは, in vivo でタイプIIカデリンに対する機能的特異性をコードします.
  • EC1ドメインのインターフェースの構造的な違いは,タイプIとタイプIIのカデリンの固着性特性に寄与する.