関連する実験動画
Updated: Jul 13, 2026

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In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 26, 2011
再結合トリスケリオンハブを使用して定義されたクラスリン組立とトリメリゼーションの規制
1Department of Pharmacy, School of Pharmacy, University of California, San Francisco 94143-0552, USA.
Cell
|October 20, 1995
まとめ
クラトリンの光鎖と特定の分子領域が,クラトリンのコート組成を調節する. この研究は,内分細胞症と臓器生物発生に不可欠なクラトリンの自己組み立てを分析するための再結合システムを確立しています.
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.
- 構造生物学 構造生物学とは
背景:
- クラトリンポリメリゼーションは,内分泌とオルゲネス生殖の間に受容体の分類に不可欠な膀のコートを形成します.
- クラトリンの自己組織化を理解することは,これらの基本的な細胞のプロセスを解明する鍵です.
研究 の 目的:
- クラトリンの自己組み立てを制御する分子メカニズムを調査する.
- クラトリンのコート形成を研究するための機能的な再結合システムを確立する.
主な方法:
- バクテリアのクラトリン重鎖のC末端の3分の1を表現した.
- 鍵となる機能ドメインを特定するために,デリション変異遺伝を活用した.
- リコンビナンスの断片のトリメリゼーション,軽鎖結合,自己組み立ての性質を分析した.
主要な成果:
- 再結合クラトリンの重鎖断片は,クラトリンの軽鎖を成功裏にトリメリゼーションし,結合させた.
- セルフ・アセンブリの研究では,クラトリンの軽鎖と遠足領域の規制作用が明らかになった.
- ライトチェーン結合と自己組み立てを媒介する特定のドメインと,移転可能なトリメリゼーションドメインが局所化されました.
結論:
- クラトリンの軽鎖と重鎖の特定の領域を含む分子相互作用は,クラトリンのコート組立に不可欠です.
- 確立された再結合系は,クラトリンの動力学と機能に関する将来の調査のための貴重なツールを提供します.
関連する概念動画
COP Coated Vesicles
Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of different...
Pinching-off of Coated Vesicles
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Coat Assembly and GTPases
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...
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...
Vesicular Tubular Clusters
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
With the help of motor proteins such...
Clathrin Coated Vesicles
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

