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Related Concept Videos

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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Rab Proteins01:14

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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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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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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.
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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.
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Recycling Endosomes and Transcytosis00:58

Recycling Endosomes and Transcytosis

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The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
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Updated: May 15, 2025

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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A competition network connects Rab5 and Rab11 GTPases at the surface of endocytic structures.

Elsi Ferro1,2, Simone Tealdi2,3, Jean Piero Margaria4,5

  • 1Department of Applied Science and Technology, Politecnico di Torino, Corso Duca degli Abruzzi 24, 10129 Turin, Italy.

Iscience
|April 9, 2025
PubMed
Summary
This summary is machine-generated.

Molecular competition between Rab GTPases for shared proteins, like Zfyve26, links membrane trafficking pathways. This competition, governed by stoichiometric constraints, regulates endocytic traffic at organelle surfaces.

Keywords:
Cell biologyFunctional aspects of cell biologyMolecular interactionOrganizational aspects of cell biology

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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Membrane trafficking specificity is traditionally attributed to unique Rab GTPase-effector interactions.
  • Emerging evidence suggests Rab proteins can interact with common effectors, challenging this specificity model.

Purpose of the Study:

  • To investigate how molecular competition among Rab GTPases for shared effectors influences membrane trafficking pathways.
  • To elucidate the role of Zfyve26 in a competitive network modulating Rab5 and Rab11 activity at endosomes.

Main Methods:

  • Theoretical modeling of molecular competition in Rab GTPase networks.
  • Experimental analysis of Rab GTPase dynamics using time-lapse imaging.
  • Development and application of the novel 'Loop index' metric to quantify Rab GTPase saturation.

Main Results:

  • Demonstrated that Zfyve26 acts as a central node in a competitive network involving Rab5 and Rab11.
  • Showed that competition modulates Rab5-Rab11 abundance, activation, and correlation on endocytic structures.
  • Quantified Zfyve26 saturation at the endocytic surface using the Loop index.

Conclusions:

  • Molecular competition among Rab GTPases for shared proteins is a key mechanism linking diverse membrane trafficking pathways.
  • Stoichiometric constraints at the organelle surface govern the trade-offs between competing trafficking routes.
  • This competitive network provides a framework for understanding signal transduction in the endocytic system.