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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...
Rab Cascades01:25

Rab Cascades

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.
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:
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...
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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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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GTPase networks in membrane traffic.

Emi Mizuno-Yamasaki1, Felix Rivera-Molina, Peter Novick

  • 1Institute for Molecular and Cellular Regulation, Gunma University, Maebashi 371-8512, Japan. eyamasak@gunma-u.ac.jp

Annual Review of Biochemistry
|April 3, 2012
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Summary

Ras GTPases, like Rab and ARF/Sar proteins, coordinate intracellular membrane traffic through complex networks. These interactions ensure organized transport by linking different stages and modifying compartment function.

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

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Published on: November 11, 2018

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

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Imaging G-protein Coupled Receptor (GPCR)-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Ras GTPases, including Rab and ARF/Sar proteins, are crucial regulators of intracellular membrane traffic.
  • These GTPases are increasingly recognized as components of intricate networks rather than isolated entities.

Purpose of the Study:

  • To elucidate the mechanisms by which Ras GTPases coordinate intracellular membrane transport.
  • To understand how these networks link different stages of transport pathways and define compartment identity.

Main Methods:

  • The study reviews existing evidence on the regulatory mechanisms of Ras GTPases.
  • Focuses on network interactions including guanine nucleotide exchange factor (GEF) and GTPase-activating protein (GAP) cascades.
  • Examines effector binding and positive-feedback loops in GTPase regulation.

Main Results:

  • Ras GTPases are networked through GEF and GAP cascades, effector interactions, and feedback loops.
  • These networks facilitate ordered transitions between different GTPases.
  • Each GTPase-effector set uniquely modifies the function of associated membrane compartments.

Conclusions:

  • Intracellular membrane traffic is orchestrated by complex, interconnected networks of Ras GTPases.
  • These networks enable precise coordination of transport stages and dynamic regulation of organelle function.
  • Understanding these GTPase networks is key to deciphering the complexities of membrane trafficking.