Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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:
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...
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...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Comment on "Comparison of the efficacy and safety of single-site laparoscopic hysterectomy with and without robotic assistance: A meta-analysis".

Journal of gynecology obstetrics and human reproduction·2026
Same author

Multitrophic interaction networks mediate biodiversity effects on ecosystem multifunctionality.

Nature communications·2026
Same author

Thermoreversible Diels-Alder Crosslinked Networks in Recycled Poly(ethylene terephthalate) for Reprocessability and Self-Healing.

Polymers·2026
Same author

Synthesis of hydrophobic hollow silica nanoparticles with synergistic structure-hydrophobicity regulation via different routes using composite silicon precursors.

Journal of colloid and interface science·2026
Same author

Intelligent quantification of Mn(VII) using a YOLO v3 artificial intelligence-driven smartphone monitoring platform based on nitrogen-doped blue fluorescence carbon dots.

The Analyst·2026
Same author

D-Dopachrome Tautomerase Regulates Synovial Fibrosis and Macrophage Polarization via NF-κB/CCL2 Signaling Pathway in Knee Osteoarthritis.

Current topics in medicinal chemistry·2026

Related Experiment Video

Updated: May 31, 2026

"Phagosome Closure Assay" to Visualize Phagosome Formation in Three Dimensions Using Total Internal Reflection Fluorescent Microscopy (TIRFM)
10:07

"Phagosome Closure Assay" to Visualize Phagosome Formation in Three Dimensions Using Total Internal Reflection Fluorescent Microscopy (TIRFM)

Published on: August 26, 2016

Rab GTPases act in sequential steps to regulate phagolysosome formation.

Pengfei Guo1, Xiaochen Wang

  • 1National Institute of Biological Sciences; Beijing, China.

Small Gtpases
|June 21, 2011
PubMed
Summary

This study reveals how Rab GTPases regulate the degradation of apoptotic cells in C. elegans. Specific Rab proteins, RAB-14 and UNC-108, recruit lysosomes, while RAB-7 mediates their fusion for efficient cell corpse clearance.

More Related Videos

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

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

Published on: November 11, 2018

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

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

Related Experiment Videos

Last Updated: May 31, 2026

"Phagosome Closure Assay" to Visualize Phagosome Formation in Three Dimensions Using Total Internal Reflection Fluorescent Microscopy (TIRFM)
10:07

"Phagosome Closure Assay" to Visualize Phagosome Formation in Three Dimensions Using Total Internal Reflection Fluorescent Microscopy (TIRFM)

Published on: August 26, 2016

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

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

Published on: November 11, 2018

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

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Apoptosis involves the engulfment of dying cells by phagocytes.
  • Phagosome maturation is crucial for the degradation of engulfed apoptotic cells.
  • The precise regulatory mechanisms governing phagosome maturation remain incompletely understood.

Purpose of the Study:

  • To identify novel regulators of apoptotic cell degradation in C. elegans.
  • To elucidate the role of Rab GTPases in phagosome maturation and function.

Main Methods:

  • Genetic analysis of C. elegans mutants.
  • Microscopy to observe phagosome dynamics and cell corpse degradation.
  • Functional studies of Rab GTPase involvement in lysosome recruitment and fusion.

Main Results:

  • C. elegans Rab GTPase 14 (rab-14) was identified as a novel regulator of apoptotic cell degradation.
  • Loss of rab-14 function leads to the accumulation of persistent cell corpses due to impaired phagosome maturation.
  • RAB-14 and UNC-108 (Rab GTPase 2) redundantly regulate phagosome maturation, with RAB-14 and UNC-108 recruiting lysosomes.
  • RAB-7 mediates the fusion of lysosomes to phagosomes, completing the process.

Conclusions:

  • Rab GTPases act sequentially to regulate lysosome tethering, docking, and fusion with phagosomes.
  • RAB-14 and UNC-108 function upstream of RAB-7 in the phagolysosome formation pathway.
  • This study reveals a cooperative mechanism involving multiple Rab GTPases in efficient apoptotic cell clearance.