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Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

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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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Coat Assembly and GTPases01:33

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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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Overview of Secretory Vesicles01:33

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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Rab Cascades01:25

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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

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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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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.
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Related Experiment Video

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Investigating Mast Cell Secretory Granules; from Biosynthesis to Exocytosis
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The Ral small GTPase is an essential regulator of Exocyst complex function in secretion.

You Wu1,2, David J Reiner1,2

  • 1College of Medicine, Texas A&M Health Science Center, Texas A&M University, Houston, TX 77030, USA.

Biorxiv : the Preprint Server for Biology
|September 5, 2025
PubMed
Summary
This summary is machine-generated.

This study shows Ral GTPase (RAL-1) directly regulates the Exocyst complex in C. elegans, impacting neuron development and vesicle transport. These findings reveal a new role for Ral in metazoan cell biology.

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

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Background:

  • The Exocyst complex is crucial for vesicle trafficking in metazoans, but its regulators are not fully understood.
  • Ral GTPases are implicated in Exocyst regulation, yet direct evidence in metazoans is limited.
  • Yeast Exocyst function involves Rab GTPases, but lacks Ral GTPases.

Purpose of the Study:

  • To investigate the direct role of Ral GTPase (RAL-1) in regulating the Exocyst complex in Caenorhabditis elegans.
  • To elucidate the molecular mechanisms and physiological consequences of RAL-1-Exocyst interactions.
  • To establish C. elegans as a model for studying Ral-Exocyst pathways.

Main Methods:

  • Utilized Caenorhabditis elegans as a model organism.
  • Employed structure-guided genome editing to probe RAL-1-Exocyst interfaces.
  • Assessed effects on neuronal development (PVD dendritic arborization) and vesicle trafficking.

Main Results:

  • Demonstrated direct engagement of endogenous RAL-1 with the Exocyst complex via conserved binding sites.
  • Showed that loss of RAL-1 leads to disrupted dendritic arborization and impaired vesicle trafficking.
  • Observed both cell-autonomous and non-autonomous effects of RAL-1, impacting neurons and epithelial cells.
  • Synthetic phenotypes generated by editing RAL-1-Exocyst interfaces confirmed functional importance.

Conclusions:

  • RAL-1 is a bona fide regulator of the metazoan Exocyst complex in vivo.
  • Ral-Exocyst interactions function independently of other secretory pathways.
  • C. elegans provides a powerful system for dissecting Ral-Exocyst mechanisms at multiple biological scales.