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

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

18.5K
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...
18.5K
Rab Cascades01:25

Rab Cascades

3.8K
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.
3.8K
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

5.3K
Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
5.3K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.8K
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...
4.8K
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

4.5K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
4.5K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

11.8K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
11.8K

You might also read

Related Articles

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

Sort by
Same author

GPR17+ Oligodendrocyte Lineage Cells Regulate the Critical Period of Brain Development Through Novel Chondroitin Sulfate-Rich Structures.

Glia·2026
Same author

Pien-Tze-Huang inhibits colorectal cancer liver metastasis in mice by modulating immunosuppressive and fibrotic microenvironments.

Translational research : the journal of laboratory and clinical medicine·2026
Same author

Integrated Network Pharmacology, Transcriptomics, and Experimental Validation Identify PI3K-AKT and STAT3 as Key Pathways for Pien Tze Huang Against Liver and Colorectal Cancers.

Current pharmaceutical design·2026
Same author

Living Polymerization of Isoprene and Synthesis of Polar Functionalized Copolymers Catalyzed by Robust Cobalt Complexes Bearing Imidazolidin-2-imine and Phosphine Ligands.

Inorganic chemistry·2025
Same author

Enhancing monoclonal antibody diversity by integrating bulk sorting and machine learning.

Biochemistry and biophysics reports·2025
Same author

CircHPCAL1 promotes the progression of pancreatic cancer via the regulation of STEAP2.

Clinical and translational medicine·2025

Related Experiment Video

Updated: Apr 20, 2026

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

9.1K

RILP interacts with HOPS complex via VPS41 subunit to regulate endocytic trafficking.

Xiaosi Lin1, Ting Yang1, Shicong Wang1

  • 1School of Pharmaceutical Sciences, State Key Laboratory of Cellular Stress Biology, Xiamen University, Xiamen, Fujian, China, 361005.

Scientific Reports
|December 3, 2014
PubMed
Summary

RILP protein interacts with the HOPS complex via VPS41, independent of Rab7, to regulate late endosomal trafficking and epidermal growth factor receptor (EGFR) degradation.

More Related Videos

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

9.5K
Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast
10:02

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast

Published on: October 23, 2016

11.5K

Related Experiment Videos

Last Updated: Apr 20, 2026

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

9.1K
Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

9.5K
Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast
10:02

Applications of pHluorin for Quantitative, Kinetic and High-throughput Analysis of Endocytosis in Budding Yeast

Published on: October 23, 2016

11.5K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Endosomal Trafficking

Background:

  • The HOPS complex is crucial for late endosomal maturation in yeast, but its mammalian function is less understood.
  • Rab7 effectors regulate endosomal pathways, yet their interactions with HOPS are not fully defined.

Purpose of the Study:

  • To investigate the interaction between RILP, a Rab7 effector, and the HOPS complex in mammalian cells.
  • To elucidate the functional role of this interaction in endocytic trafficking.

Main Methods:

  • Co-immunoprecipitation assays to detect protein interactions.
  • Depletion of VPS41 using shRNA and overexpression of VPS41 fragments.
  • Analysis of Epidermal Growth Factor Receptor (EGFR) degradation.

Main Results:

  • RILP directly interacts with the HOPS complex, recruiting it to late endosomes.
  • The N-terminal region of RILP binds the C-terminal region of VPS41, independent of Rab7.
  • VPS41 depletion or overexpression of its C-terminal half impairs EGFR degradation.

Conclusions:

  • RILP-HOPS interaction via VPS41 is a novel mechanism regulating late endosomal function.
  • This interaction plays a significant role in the endocytic trafficking and degradation of EGFR.