関連する実験動画
Updated: May 8, 2026

09:58
RhoC GTPase Activation Assay
Published on: August 23, 2010
GTPaseダイナミンは,SH3ドメインのサブセットと結合し,活性化されます
Cell
|October 8, 1993
まとめ
Srcホモロジー3 (SH3) ドメインは,プロリン豊富なモチーフを介してGTPaseダイナミンと結合する. この相互作用は,タンパク質とタンパク質の結合を促進するだけでなく,ダイナミンを調節します.
科学分野:
- 分子生物学は分子生物学である.
- 細胞シグナリング 細胞シグナリング
- タンパク質の相互作用
背景:
- Srcホモロジー3 (SH3) ドメインは,細胞シグナル伝達経路におけるタンパク質対タンパク質の相互作用に不可欠である.
- SH3ドメインの正確な機能,特にGTP結合タンパク質との関係については,さらなる解明が必要である.
研究 の 目的:
- SH3ドメインと相互作用するタンパク質を特定する.
- GTPase活性に対するSH3ドメイン結合の機能的影響を調査する.
主な方法:
- SH3ドメイン結合タンパク質を分離するために,アフィニティ浄化技術を使用した.
- 再結合SH3ドメインは,選択的結合相互作用を研究するために使用されました.
- GTPase活性アッセイは,機能的調節を評価するために実施されました.
主要な成果:
- GTPaseダイナミンは,新しいSH3ドメイン結合タンパク質として特定されました.
- 結合はプロリンに富んだ配列モチーフを通じて発生し,既知のSH3相互作用に類似しています.
- いくつかのSH3ドメインがダイナミンのGTPase活性を刺激することが判明しました.
結論:
- SH3ドメインは,ダイナミンと特定のタンパク質の相互作用を媒介する.
- SH3ドメインの機能は,単純な結合を超えて,GTP結合タンパク質の活性を調節することを含む.
- これらの発見は,受容体シグナル伝達とGTPase調節におけるSH3ドメインの役割に関する新しい洞察を提供します.
関連する概念動画
GTPases and their Regulation
Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒ small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
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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...
GTPases and their Regulation
Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒ small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
Large G-proteins, also known...
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,...
Small GTPases - Ras and Rho
Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
Three regulatory proteins control their activity:
Activation and Inactivation of G Proteins
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...

