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相关概念视频

Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

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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:
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GTPases and their Regulation02:14

GTPases and their Regulation

8.2K
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,...
8.2K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

6.6K
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...
6.6K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.7K
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,...
5.7K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

8.2K
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...
8.2K
Rab Cascades01:25

Rab Cascades

2.6K
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.
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相关实验视频

Updated: May 27, 2025

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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分裂小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, Emily Hyun1

  • 1Department of Chemistry, University of Virginia, Charlottesville, VA 22904, USA.

bioRxiv : the preprint server for biology
|February 20, 2025
PubMed
概括

研究人员开发了一种plug-and-play方法,使用分裂GTPase和化学诱导二元化 (CID) 来控制小GTPase信号传输. 这允许精确的时间操纵细胞功能,如迁移和增殖.

更多相关视频

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Comparing the Affinity of GTPase-binding Proteins using Competition Assays

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

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相关实验视频

Last Updated: May 27, 2025

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

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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科学领域:

  • 分子生物学分子生物学
  • 细胞信号传递 细胞信号传递
  • 生物化学 生化学

背景情况:

  • 小GTPases调节关键的细胞过程,包括迁移和增殖.
  • 目前的方法缺乏对小GTPase活动的直接时间控制,阻碍了研究.
  • 需要一个插即用系统来精确操纵GTPase信号.

研究的目的:

  • 开发一种多功能,插即用的方法,用于直接,暂时控制小GTPase活动.
  • 为了实现用户定义的输入来调节特定的蜂信号通路.
  • 克服在活细胞中剖析GTPase功能的局限性.

主要方法:

  • 开发了可以使用化学二元化诱导剂 (CID) 重组的分裂GTPase系统.
  • 配对分割GTPase与各种CID系统进行模块化控制.
  • 应用该系统来研究MAPK信号传递,类动物的形成和细胞收缩.

主要成果:

  • 展示了用于直接控制小GTPase信号的直接时间控制的插入式操作方法.
  • 通过使用不同的CID系统来展示模块化,最小的目标外影响.
  • 实现了控制MAPK信号传递,类动物和细胞收缩的一致通路激活.

结论:

  • 分割GTPase系统提供了一个可定制的平台,用于精确的时间控制蜂信号.
  • 这种方法允许用户定义的GTPase活性调节,途径干扰最小.
  • 提供了一种新的工具,用于在不同的生物环境中研究GTPase功能.