Related Experiment Video

Updated: Jun 11, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Coro1a promotes the multivesicular body and plasma membrane fusion by facilitating PKM2-mediated SNAP-23

Zhenzhai Cai1, Zhijie Li2, Nannan Li1

  • 1Department of Gastroenterology, the Second Affiliated Hospital and Yuying Children's Hospital of Wenzhou Medical University, Wenzhou, China.

Communications Biology
|June 9, 2026
PubMed

Insights

Coronin-1a promotes extracellular vesicle (EV) release by enhancing SNARE complex assembly, independent of neddylation. This process involves activating PKM2 to drive EV biogenesis, which is crucial for tumor progression.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Exosome release occurs via multivesicular bodies (MVBs) fusing with the plasma membrane (PM).
  • The soluble N-ethyl-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex drives this fusion.
  • The specific SNARE complex and regulatory mechanisms for MVB-PM fusion are not fully understood.

Purpose of the Study:

  • To elucidate the role of Coronin-1a (Coro1a) in extracellular vesicle (EV) biogenesis.
  • To identify the specific SNARE complex involved in MVB-PM fusion mediated by Coro1a.
  • To investigate the mechanism by which Coro1a regulates EV production and its implications in cancer.

Main Methods:

  • Investigated the effect of Coronin-1a (Coro1a) on extracellular vesicle (EV) biogenesis.
  • Utilized techniques to analyze SNARE complex assembly (STX-12-SNAP-23-VAMP-7).
  • Examined the role of pyruvate kinase M2 (PKM2) and SNAP-23 phosphorylation in Coro1a-mediated EV production.
  • Assessed Coro1a levels in lung tumor tissues and correlated them with patient survival.

Main Results:

  • Coronin-1a (Coro1a) promotes extracellular vesicle (EV) biogenesis by facilitating the STX-12-SNAP-23-VAMP-7 SNARE complex assembly.
  • Coro1a activates pyruvate kinase M2 (PKM2), enhancing SNAP-23 phosphorylation and recruiting STX-12 and VAMP-7.
  • Coro1a-induced EV biogenesis was abrogated by PKM2 inhibition or SNAP-23 silencing.
  • Elevated Coro1a levels in lung tumors correlated with poorer patient survival.

Conclusions:

  • Coronin-1a (Coro1a) is a key regulator of EV biogenesis through SNARE complex assembly during MVB-PM fusion.
  • The Coro1a-PKM2-SNAP-23 pathway enhances EV production, contributing to tumor progression.
  • Coro1a represents a potential therapeutic target in cancers where EV production is implicated.

More Related Videos

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays08:27

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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...
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

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...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...