SNARE-mediated membrane fusion

  title={SNARE-mediated membrane fusion},
  author={Yu A. Chen and Richard H. Scheller},
  journal={Nature Reviews Molecular Cell Biology},
SNARE proteins have been proposed to mediate all intracellular membrane fusion events. There are over 30 SNARE family members in mammalian cells and each is found in a distinct subcellular compartment. It is likely that SNAREs encode aspects of membrane transport specificity but the mechanism by which this specificity is achieved remains controversial. Functional studies have provided exciting insights into how SNARE proteins interact with each other to generate the driving force needed to fuse… 

SNARE proteins in membrane trafficking

An update on the recent progress on SNAREs regulating membrane fusion events, especially the more detailed fusion processes dissected by well‐developed biophysical methods and in vitro single molecule analysis approaches is provided.

Regulated exocytosis and SNARE function (Review)

The pairing of cognate v- and t-SNAREs between two opposing lipid bilayers drives spontaneous membrane fusion and confers specificity to intracellular membrane trafficking. These fusion events are

Three SNARE complexes cooperate to mediate membrane fusion

  • Yuanyuan HuaR. Scheller
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 2001
The increase in the inhibition of fusion observed with increasing concentration of inhibitor is best fit to a function that suggests three SNARE complexes cooperate to mediate fusion of a single vesicle.

SNARE protein structure and function.

The SNARE superfamily has become, since its discovery approximately a decade ago, the most intensively studied element of the protein machinery involved in intracellular trafficking and there is still much to learn about how the assembly and activity of this machinery is choreographed in living cells.

The syntaxins

SUMMARY The SNARE hypothesis predicts that a family of SNAP receptors are localized to and function in diverse intracellular membrane compartments where membrane fusion processes take place.

A reduced SNARE model for membrane fusion.

A minimal model system was developed to mimic the SNARE-protein-mediated fusion of biological membranes and displays the key characteristics of in vivo fusion events.

Multiple ER–Golgi SNARE transmembrane domains are dispensable for trafficking but required for SNARE recycling

Yeast cells in which a particular essential ER–Golgi SNARE’s transmembrane domain has been removed remain viable and devoid of forward-trafficking defects.

A new catch in the SNARE.

Selective Activation of Cognate SNAREpins by Sec1/Munc18 Proteins




SNAREpins: Minimal Machinery for Membrane Fusion

Compartmental specificity of cellular membrane fusion encoded in SNARE proteins

It is found that, to a marked degree, the pattern of membrane flow in the cell is encoded and recapitulated by its isolated SNARE proteins, as predicted by the SNARE hypothesis.

Transport-vesicle targeting: tethers before SNAREs

Despite the wide diversity in the identities of the players, some common themes are emerging that may explain how vesicles can identify their targets and release their cargo at the correct time and place in eukaryotic cells.

Topological restriction of SNARE-dependent membrane fusion

Each SNARE protein is topologically restricted by design to function either as a v- SNARE or as part of a t-SNARE complex, and reconstituted two populations of phospholipid bilayer vesicles, with the individual SNARE proteins distributed in all possible combinations between them.

Functional architecture of an intracellular membrane t-SNARE

Here it is shown that an intracellular t-SNARE is built from a ‘heavy chain’ homologous to syntaxin and two separate non-syntaxin ‘light chains’.

Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs.

A fusion assay that relies on duplex formation of oligonucleotides introduced in separate liposome populations is used and it is reported that SNARE proteins suffice to mediate complete membrane fusion accompanied by mixing of luminal content and thatSNARE-mediated membrane fusion does not compromise the integrity of liposomes.

Defining the functions of trans-SNARE pairs

Data indicate that SNARE pairing may transiently signal to downstream factors, leading to fusion of yeast vacuoles, as the function of this trans-SNARE complex must be transient.

Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP

It is reported that SNAREpins (trans-SNARE complexes) are in fact functionally resistant to NSF, and they become so at the moment they form and commit to fusion, which allows fusion to proceed locally in the face of an overall environment that massively favors SNARE disruption.