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 Proteins01:14

Rab Proteins

3.9K
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...
3.9K
Rab Cascades01:25

Rab Cascades

2.6K
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.
2.6K
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

3.9K
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:
3.9K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

3.5K
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...
3.5K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

7.2K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
7.2K
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

2.5K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
2.5K

You might also read

Related Articles

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

Sort by
Same author

Avl9 defines a family of GTPase-activating proteins that regulate diverse cell biological functions.

bioRxiv : the preprint server for biology·2026
Same author

Tetraspanin TSP-12 and SUP-17/ADAM10 exhibit cell type-specific codependence for trafficking through the Golgi.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

The Inaugural Flatiron Institute Cryo-EM Conformational Heterogeneity Challenge.

bioRxiv : the preprint server for biology·2025
Same author

Atg2/TRAPPIII-Ypt1 axis: deciphering the phagophore-ERES connection.

Autophagy·2025
Same author

Female membrane proteins regulate postmating ovulation in <i>Drosophila melanogaster</i> by ovulin-dependent and -independent pathways.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Establishment of the phagophore-ERES membrane contact site initiates phagophore elongation.

Nature structural & molecular biology·2025

Related Experiment Video

Updated: Jun 26, 2025

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using &#967;CRAC
09:15

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

5.0K

Structural basis for Rab6 activation by the Ric1-Rgp1 complex.

J Ryan Feathers1,2, Ryan C Vignogna1, J Christopher Fromme1

  • 1Department of Molecular Biology & Genetics and Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14850 USA.

Biorxiv : the Preprint Server for Biology
|May 20, 2024
PubMed
Summary

Researchers uncovered the structure of a key protein complex that activates Rab6, a molecule crucial for organelle function. This finding reveals novel mechanisms for regulating membrane trafficking within cells.

More Related Videos

Study of Protein-protein Interactions in Autophagy Research
14:08

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

9.1K
Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE
12:43

Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE

Published on: July 29, 2014

12.1K

Related Experiment Videos

Last Updated: Jun 26, 2025

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using &#967;CRAC
09:15

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

5.0K
Study of Protein-protein Interactions in Autophagy Research
14:08

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

9.1K
Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE
12:43

Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE

Published on: July 29, 2014

12.1K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • Rab GTPases are essential regulators of organelle homeostasis and membrane trafficking.
  • Rab6 specifically controls Golgi apparatus cargo flux, activated by the conserved Ric1-Rgp1 protein complex.
  • The structural and mechanistic basis of Ric1-Rgp1 function remained unelucidated.

Conclusions:

  • The study provides a detailed mechanistic understanding of Rab6 activation at the Golgi.
  • Novel insights into the structural basis of RabGEF function and Rab GTPase regulation were revealed.
  • The findings suggest that arrestin-like folds may commonly mediate interactions with Rab GTPase C-terminal regions.