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

COP Coated Vesicles00:59

COP Coated Vesicles

7.9K
Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
7.9K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

3.6K
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...
3.6K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

7.3K
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...
7.3K
Rab Proteins01:14

Rab Proteins

4.0K
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...
4.0K
Regulated mRNA Transport02:22

Regulated mRNA Transport

2.8K
2.8K
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

4.0K
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:
4.0K

You might also read

Related Articles

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

Sort by
Same author

Seventh Åland Island Meeting on von Willebrand Disease.

Haemophilia : the official journal of the World Federation of Hemophilia·2026
Same author

UBB as an early-stage potential biomarker for breast cancer via modulation of the ubiquitination pathway.

Scientific reports·2026
Same author

Epidermal deletion of Kindlin-1 drives matrix changes in the mouse skin and altered responses to ultraviolet radiation.

Journal of dermatological science·2026
Same author

Tissue-specific fibroblast lipid cues impose the rate of epithelial cancer invasion.

Nature metabolism·2026
Same author

The lipid transfer protein STARD7 controls intestinal tumor development in a context-dependent manner.

EMBO molecular medicine·2026
Same author

The Role of A-Kinase Anchoring Proteins for Inhibitory cAMP Signalling in Platelets.

Cells·2026

Related Experiment Video

Updated: Jul 24, 2025

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

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

9.2K

RhoGAP6 interacts with COPI to regulate protein transport.

Lorna O'Donoghue1,2, Shane P Comer1,2, Dishon W Hiebner2,3

  • 1UCD School of Medicine, Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield Dublin 4, Ireland.

The Biochemical Journal
|July 6, 2023
PubMed
Summary

Platelet RhoGAP6 interacts with δ-COP via di-tryptophan motifs, influencing protein transport without affecting RhoA activity. This novel RhoGAP6-δ-COP interaction connects RhoGAP6 to the COPI complex, impacting platelet function.

Keywords:
ARHGAP6G-proteinsRhoAintracellular transportplatelets

More Related Videos

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
10:53

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution

Published on: January 16, 2017

9.1K
Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip
13:34

Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

Published on: September 29, 2012

27.6K

Related Experiment Videos

Last Updated: Jul 24, 2025

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

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

9.2K
Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
10:53

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution

Published on: January 16, 2017

9.1K
Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip
13:34

Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

Published on: September 29, 2012

27.6K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Platelet Biology

Background:

  • RhoGAP6 is the primary RhoA-specific GTPase-activating protein in platelets.
  • Its structure includes a catalytic GAP domain and disordered termini with unknown functions.
  • Conserved di-tryptophan motifs near the C-terminus suggest potential interactions with COPI complex components.

Purpose of the Study:

  • To investigate the functional role of RhoGAP6's C-terminal motifs.
  • To identify and characterize binding partners of RhoGAP6.
  • To elucidate the impact of RhoGAP6 interactions on platelet protein transport and RhoA activity.

Main Methods:

  • Sequence analysis to identify conserved motifs.
  • Co-immunoprecipitation and GST pull-down assays to confirm protein interactions.
  • Site-directed mutagenesis to map binding sites.
  • Proteomic analysis to identify binding partners.
  • Analysis of protein transport via the secretory pathway.

Main Results:

  • Confirmed an endogenous interaction between RhoGAP6 and δ-COP in human platelets.
  • Demonstrated that RhoGAP6 di-tryptophan motifs and δ-COP's mu homology domain mediate this interaction.
  • Identified 14-3-3 as another RhoGAP6 binding partner.
  • Found that RhoGAP6/δ-COP binding enhances protein transport to the plasma membrane, independent of RhoA activity.

Conclusions:

  • A novel interaction between RhoGAP6 and δ-COP, mediated by C-terminal di-tryptophan motifs, has been identified.
  • This interaction links RhoGAP6 to the COPI complex and influences protein transport in platelets.
  • The RhoGAP6-δ-COP interaction may play a regulatory role in platelet secretion and function.