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Related Concept Videos

Rab Proteins01:14

Rab Proteins

4.8K
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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Rab Cascades01:25

Rab Cascades

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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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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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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.1K
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...
4.1K
GTPases and their Regulation02:14

GTPases and their Regulation

9.6K
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,...
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GTPases and their Regulation02:14

GTPases and their Regulation

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Related Experiment Video

Updated: Dec 19, 2025

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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A non-linear system patterns Rab5 GTPase on the membrane.

Alice Cezanne1, Janelle Lauer1, Anastasia Solomatina1,2,3

  • 1Max-Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.

Elife
|June 9, 2020
PubMed
Summary

Small GTPase Rab5 proteins self-organize into membrane patterns. This patterning requires specific lipid compositions and involves a GEF/effector complex, suggesting a universal mechanism for protein self-organization.

Keywords:
GTPase domainRab5biochemistrychemical biologyendocytosisnonepattern formationreconstitutionself-organization

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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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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Area of Science:

  • Cellular Biology
  • Biophysics
  • Systems Biology

Background:

  • Small GTPases are key regulators of cellular processes.
  • Protein self-organization into spatial patterns is crucial for cellular function.
  • Previous modeling suggested GTPase-GEF-effector interactions drive patterning.

Purpose of the Study:

  • To reconstitute and analyze the patterning of small GTPase Rab5 on lipid bilayers.
  • To elucidate the roles of GEF/effector complexes and lipid composition in Rab5 patterning.
  • To investigate the mechanism of Rab5 recruitment and domain formation.

Main Methods:

  • Reconstitution of Rab5 patterning on supported lipid bilayers.
  • Utilizing a minimal system of Rab5, RabGDI, and Rabex5/Rabaptin5 complex.
  • Varying lipid membrane composition to mimic early endosomes.

Main Results:

  • Demonstrated a 'handover' mechanism of Rab5 between GEF (Rabex5) and effector (Rabaptin5).
  • Identified a minimal system required for Rab5 membrane domain patterning.
  • Showcased the importance of PI(3)P and lipid acyl chain packing for Rab5 recruitment and domain formation.

Conclusions:

  • Rab5 patterning is driven by a combination of protein-protein interactions and specific lipid membrane properties.
  • The study reveals a potential universal mechanism for small GTPase patterning involving protein and lipid interplay.
  • Findings provide insights into the fundamental principles of protein self-organization in biological membranes.