相关实验视频
Updated: May 8, 2026

09:58
RhoC GTPase Activation Assay
Published on: August 23, 2010
GTPase动氨酸与SH3域的一个子集结合并被激活
Cell
|October 8, 1993
概括
Src同质性3 (SH3) 域通过富含proline的基因与GTPasedynamin结合. 这种相互作用不仅促进了蛋白质与蛋白质的结合,而且还调节了动氨酸.
科学领域:
- 分子生物学分子生物学
- 细胞信号传递 细胞信号传递
- 蛋白相互作用 蛋白相互作用
背景情况:
- Src同质性3 (SH3) 域对于细胞信号通路中的蛋白质-蛋白质相互作用至关重要.
- SH3域的确切功能,特别是与GTP结合蛋白相关的功能,需要进一步阐明.
研究的目的:
- 识别与SH3域相互作用的蛋白质.
- 为了研究SH3域结合对GTPase活性的功能后果.
主要方法:
- 采用了亲和性净化技术来分离SH3域结合蛋白.
- 再组合的SH3域被用于研究选择性结合相互作用.
- 进行了GTPase活性测定以评估功能调节.
主要成果:
- 鉴定出GTPasedynamin是一种新的SH3域结合蛋白.
- 结合是通过富含proline的序列动机发生的,类似于已知的SH3相互作用.
- 发现多个SH3域刺激了dynamin的GTPase活性.
结论:
- SH3 域调解特定的蛋白质与蛋白质相互作用.
- SH3域的功能超出了简单的结合范围,包括调节GTP结合蛋白活性.
- 这些发现为SH3域在受体信号传递和GTPase调节中的作用提供了新的见解.
相关概念视频
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...
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...

