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SNAREs and Membrane Fusion

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 Membrane

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...

Formation of Intermediate Filaments

Formation of Intermediate Filaments

Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.

Viral Recombination

Viral Recombination

Cells are sometimes infected by more than one virus at once. When two viruses disassemble to expose their genomes for replication in the same cell, similar regions of their genomes can pair together and exchange sequences in a process called recombination. Alternatively, viruses with segmented genomes can swap segments in a process called reassortment.

Vesicular Tubular Clusters

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.
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Viral Structure

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Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.

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Related Experiment Video

Updated: May 12, 2026

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

Published on: September 14, 2014

Intermediate conformations during viral fusion glycoprotein structural transition.

Eduard Baquero¹, Aurélie A Albertini, Patrice Vachette

¹Centre de Recherche de Gif, Laboratoire de Virologie Moléculaire et Structurale, CNRS (UPR 3296), 91198 Gif sur Yvette Cedex, France.

Current Opinion in Virology

|April 9, 2013

Summary

Viral glycoproteins mediate cell entry by driving membrane fusion through conformational changes. This review highlights data supporting a pre-hairpin intermediate, though its structure remains debated.

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Last Updated: May 12, 2026

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Published on: September 14, 2014

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Determination of Molecular Structures of HIV Envelope Glycoproteins using Cryo-Electron Tomography and Automated Sub-tomogram Averaging

Determination of Molecular Structures of HIV Envelope Glycoproteins using Cryo-Electron Tomography and Automated Sub-tomogram Averaging

Published on: December 1, 2011

Area of Science:

Virology
Structural Biology
Biochemistry

Background:

Enveloped viruses enter cells via membrane fusion, a process mediated by viral glycoproteins.
Three classes of viral fusion proteins are known, with distinct structural and functional properties.
Static crystal structures reveal pre- and post-fusion states but not the dynamic transition pathway.

Purpose of the Study:

To review recent data characterizing intermediate structures during viral fusion protein conformational changes.
To elucidate the transition pathway of viral glycoproteins during membrane fusion.
To discuss the oligomeric status of the pre-hairpin intermediate.

Main Methods:

Review of recent structural and biophysical studies.
Analysis of data on viral glycoprotein conformational dynamics.
Comparative analysis of different viral fusion protein classes.

Main Results:

Evidence supports the existence of a pre-hairpin intermediate during the fusion process.
The transition pathway involves significant molecular reorganization.
The oligomeric state of the pre-hairpin intermediate is currently under investigation and debate.

Conclusions:

Understanding viral fusion intermediates is crucial for developing antiviral strategies.
The pre-hairpin intermediate is a key stage in viral membrane fusion.
Further research is needed to resolve the oligomeric status and dynamics of this intermediate.