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Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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

Fusion of Secretory Vesicles with the Plasma Membrane

19.2K
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...
19.2K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

4.0K
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...
4.0K
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

7.1K
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...
7.1K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

10.7K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
10.7K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

3.3K
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...
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Related Experiment Video

Updated: Mar 8, 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

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Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

Peng Yue1, Yubo Zhang2, Kunrong Mei1

  • 1Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.

Nature Communications
|January 24, 2017
PubMed
Summary

Sec3 protein initiates SNARE complex assembly, a key step in membrane fusion during exocytosis. This interaction, mediated by the exocyst complex, is crucial for vesicle trafficking and cellular secretion.

More Related Videos

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

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Related Experiment Videos

Last Updated: Mar 8, 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

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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Soluble N-ethylmaleimide-sensitive factor-attachment protein receptors (SNAREs) mediate membrane fusion in eukaryotic vesicular transport.
  • The initial steps and regulation of SNARE complex assembly remain largely unknown.
  • The exocyst complex is known to mediate vesicle tethering during exocytosis.

Purpose of the Study:

  • To elucidate the mechanism initiating SNARE complex assembly.
  • To investigate the role of the exocyst component Sec3 in SNARE complex formation and membrane fusion.
  • To understand how Sec3 influences the t-SNARE protein Sso2.

Main Methods:

  • Co-immunoprecipitation to detect protein interactions.
  • In vitro membrane fusion assays.
  • Crystal structure determination of the Sec3-Sso2 complex.
  • Genetic disruption of Sec3-Sso2 interaction in vivo.

Main Results:

  • Sec3 directly interacts with the t-SNARE protein Sso2.
  • This interaction promotes the formation of the Sso2-Sec9 binary t-SNARE complex, a rate-limiting step.
  • Sec3 binding induces conformational changes in Sso2, relieving its auto-inhibition and stimulating membrane fusion.
  • Disruption of the Sec3-Sso2 interaction impairs exocytosis but not Sec3's tethering function.

Conclusions:

  • Sec3 acts as an activator of SNARE complex assembly, promoting membrane fusion.
  • The exocyst complex plays a dual role in exocytosis: vesicle tethering and promoting membrane fusion.
  • This study reveals a novel mechanism for regulating SNARE-mediated membrane fusion via the exocyst.