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Related Concept Videos

Small GTPases - Ras and Rho01:24

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:
GTPases and their Regulation02:14

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...
GTPases and their Regulation02:14

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...
Coat Assembly and GTPases01:33

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...
Activation and Inactivation of G Proteins01:22

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...
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...

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Related Experiment Video

Updated: Jun 8, 2026

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

LOV conquers (sm)All GTPases.

Rachelle Kosoff, Jonathan Chernoff

    F1000 Biology Reports
    |October 16, 2010
    PubMed
    Summary
    This summary is machine-generated.

    Researchers developed a light-activated enzyme for precise control over the Rac1 GTPase. This tool allows detailed analysis of effector proteins and signaling pathways, advancing our understanding of cellular functions.

    More Related Videos

    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

    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

    Related Experiment Videos

    Last Updated: Jun 8, 2026

    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

    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

    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

    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • Subcellular localization of GTPases is crucial for their function.
    • Understanding spatial patterning of GTPases is key to deciphering protein activity.

    Purpose of the Study:

    • To develop a novel method for precise spatiotemporal control of GTPase activity.
    • To investigate the role of effector proteins in Rac1 signaling.

    Main Methods:

    • Creation of a genetically encoded, light-activated enzyme.
    • Application of the enzyme for controlling the small GTPase, Rac1.

    Main Results:

    • Achieved precise temporal and spatial control over Rac1 activity using light activation.
    • Enabled analysis of effector protein involvement in Rac1-mediated signaling.

    Conclusions:

    • The developed reagent offers a powerful tool for studying GTPase function.
    • This approach has potential applications for investigating other signaling proteins and pathways.