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相关概念视频

GTPases and their Regulation02:14

GTPases and their Regulation

8.6K
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,...
8.6K
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

4.2K
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:
4.2K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

7.6K
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...
7.6K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

8.7K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
8.7K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.9K
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,...
5.9K
Rab Cascades01:25

Rab Cascades

2.7K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
2.7K

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相关实验视频

Updated: Sep 10, 2025

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

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分离小GTPase重组作为一种控制用户定义输入的细胞信号的方法

Yuchen He1, Benjamin M Faulkner1, Rachel S Weatherford1

  • 1Department of Chemistry, University of Virginia, Charlottesville, Virginia 22904, United States.

ACS chemical biology
|August 26, 2025
PubMed
概括

研究人员开发了一种插入和操作的方法,以使用化学二元化诱导剂 (CID) 控制小三酸盐 (GTP) 酶活性. 这种系统允许精确的时间控制细胞信号通路.

更多相关视频

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Published on: November 11, 2018

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相关实验视频

Last Updated: Sep 10, 2025

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

9.3K
Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

10.9K
Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

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科学领域:

  • 分子生物学
  • 细胞信号传输
  • 生物化学

背景情况:

  • 小GTPases是调节细胞功能,如迁移和增殖的关键信号酶.
  • 目前的方法缺乏对小GTPase活动的直接时间控制,阻碍了研究.
  • 了解小GTPase角色需要精确的工具来操纵它们的信号.

研究的目的:

  • 开发用于直接控制小GTPase活动的插入式操作方法.
  • 使用户定义的输入能够精确调节蜂信号通路.
  • 为研究小GTPase函数创建一个可定制的平台.

主要方法:

  • 用化学诱导二元化 (CID) 系统对接小GTPase.
  • 使用小型GTPase系统的模块化进行CID选择.
  • 在活细胞中实现控制特定信号通路的系统.

主要成果:

  • 展示了用于直接控制小GTPase信号的插入和运行方法.
  • 展示了使用各种CID系统的一致路径激活.
  • 成功控制了MAPK信号传递,细胞的形成和细胞收缩.

结论:

  • 分离小GTPase系统提供了一个可定制的平台来控制细胞信号传输.
  • 这种方法允许使用用户定义的输入精确操纵小GTPase活动.
  • 为剖析小GTPase在各种细胞过程中的作用提供了有价值的工具.