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Related Concept Videos

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...
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:
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...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...

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

Published on: March 9, 2012

Regulating Rap small G-proteins in time and space.

Martijn Gloerich1, Johannes L Bos

  • 1Molecular Cancer Research, Centre for Biomedical Genetics and Cancer Genomics Centre, University Medical Center Utrecht, Utrecht, The Netherlands.

Trends in Cell Biology
|August 9, 2011
PubMed
Summary

Small G-protein Rap signaling is tightly regulated by Guanine nucleotide Exchange Factors (GEFs) and GTPase Activating Proteins (GAPs). These proteins control Rap

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Development and Application of Rapamycin-regulated Tyrosine Phosphatases
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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

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Development and Application of Rapamycin-regulated Tyrosine Phosphatases
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Development and Application of Rapamycin-regulated Tyrosine Phosphatases

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Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Protein Regulation

Background:

  • Small G-protein Rap signaling is crucial for various cellular processes.
  • Rap signaling is precisely controlled by Guanine nucleotide Exchange Factors (GEFs) and GTPase Activating Proteins (GAPs).
  • These regulatory proteins are themselves subject to complex upstream control and localization mechanisms.

Purpose of the Study:

  • To review the activating signals for RapGEFs and RapGAPs.
  • To discuss the targeting mechanisms that localize RapGEFs and RapGAPs within the cell.
  • To explore how these regulatory proteins contribute to the spatiotemporal control and biological functions of Rap proteins.

Main Methods:

  • Literature review of existing research on Rap signaling.
  • Analysis of upstream pathways controlling RapGEFs and RapGAPs.
  • Examination of protein anchoring mechanisms and their impact on localization.
  • Discussion of the functional consequences of Rap spatiotemporal regulation.

Main Results:

  • RapGEFs and RapGAPs act as key regulators of Rap signaling.
  • Diverse upstream pathways converge on RapGEFs and RapGAPs.
  • Multiple anchoring mechanisms ensure specific cellular localization of RapGEFs and RapGAPs.
  • Localization dictates the control of distinct Rap protein pools.

Conclusions:

  • RapGEFs and RapGAPs provide critical spatiotemporal control over Rap signaling.
  • Understanding these regulatory mechanisms is essential for elucidating Rap's diverse biological roles.
  • Targeting these regulators offers potential therapeutic strategies for diseases involving Rap dysregulation.