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

Role of Septins01:02

Role of Septins

2.2K
Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
2.2K
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

13.0K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
13.0K
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

19.1K
Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
19.1K
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

9.6K
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.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
9.6K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

3.9K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.9K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

3.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
3.4K

You might also read

Related Articles

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

Sort by
Same author

Characterizing the Fate of Anti-CS1 Nanobody Displaying Extracellular Vesicles in Multiple Myeloma.

Journal of extracellular vesicles·2026
Same author

A Syndecan-Based Genetic Approach to Coat the Surface of Small Extracellular Vesicles With Nanobodies.

Journal of extracellular biology·2026
Same author

SLAP controls mTORC2 integrity via UBE3C-mediated non-degradative mLST8 ubiquitination to suppress colorectal tumorigenesis.

Cell death and differentiation·2025
Same author

Pharmacological inhibition of myostatin effectively ameliorates osteolytic lesions in syngeneic and xenograft breast cancer mouse models.

Oncogene·2025
Same author

Syntenin Controls Extracellular Vesicle-Induced Tumour Migration by Regulating the Expression of Adhesion Proteins on Small Extracellular Vesicles.

Journal of extracellular vesicles·2025
Same author

Syntenin inhibition impairs stroma-tumor communication in multiple myeloma and improves bortezomib treatment efficiency.

HemaSphere·2025

Related Experiment Video

Updated: Feb 19, 2026

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers
10:28

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers

Published on: December 6, 2019

8.3K

Syntenin mediates SRC function in exosomal cell-to-cell communication.

Naga Sailaja Imjeti1,2,3,4, Kerstin Menck2,3,4, Antonio Luis Egea-Jimenez1,2,3,4

  • 1Department of Human Genetics, K. U. Leuven, B-3000 Leuven, Belgium.

Proceedings of the National Academy of Sciences of the United States of America
|November 8, 2017
PubMed
Summary

The cytoplasmic tyrosine kinase SRC controls exosome biogenesis and activity, promoting cell migration. This discovery reveals SRC

Keywords:
ARF6SRCexosomesyndecansyntenin

More Related Videos

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

4.0K
Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
11:50

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

2.6K

Related Experiment Videos

Last Updated: Feb 19, 2026

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers
10:28

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers

Published on: December 6, 2019

8.3K
Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

4.0K
Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
11:50

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

2.6K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Cytoplasmic tyrosine kinase SRC is known to regulate cell growth, proliferation, adhesion, and motility, primarily downstream of cell-surface receptors.
  • Exosomes, endosome-derived vesicles, play a crucial role in intercellular communication by reprogramming recipient cells.

Purpose of the Study:

  • To investigate the role of SRC in exosome biogenesis and activity.
  • To elucidate the mechanism by which SRC influences exosome-mediated cell-to-cell communication.

Main Methods:

  • Gain- and loss-of-function studies were employed to assess SRC's role in exosome secretion.
  • Investigated the involvement of syntenin, ARF6 GTPase, and phospholipase D2 in SRC-mediated exosome function.
  • Analyzed the phosphorylation of syndecan and syntenin by SRC.

Main Results:

  • SRC stimulates the secretion of exosomes with promigratory activity on endothelial cells.
  • Syntenin is essential for SRC's exosomal function.
  • SRC directly phosphorylates syndecan and syntenin, impacting endocytosis and endosomal budding.

Conclusions:

  • SRC plays a novel role in cell-cell communication through the regulation of exosome biogenesis and activity.
  • SRC-syntenin exosomes contribute to endothelial cell migration and may be involved in tumor-host interactions.