The specifics of membrane fusion

The ability to maintain a diverse set of intracellular compartments, with distinct complements of proteins, is a defining feature of eukaryotic cells. Substances can be transported from one membrane-encased compartment to another, but the compartments maintain their unique identities. Transport occu...

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Bibliographic Details
Published in:Nature (London) 2000-09, Vol.407 (6801), p.144-146
Main Authors: Scales, S J, Bock, J B, Scheller, R H
Format: Article
Language:English
Subjects:
Biological Transport
Membrane Fusion
Membrane Proteins - chemistry
Membrane Proteins - physiology
Protein Conformation
SNARE complex
SNARE Proteins
Vesicular Transport Proteins
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Summary:The ability to maintain a diverse set of intracellular compartments, with distinct complements of proteins, is a defining feature of eukaryotic cells. Substances can be transported from one membrane-encased compartment to another, but the compartments maintain their unique identities. Transport occurs in membrane-bounded containers called vesicles, and several proteins families have evolved to mediate the budding of a vesicle from the donor compartment, and its transport to and fusion with the target organelle. One of the last steps in the fusion process is overseen by a set of proteins called SNAREs. These have been suggested to be the core machinery that mediates the fusing of two membranes, as well as ensuring that vesicles deliver their cargo to the right compartment. Rothman and colleagues conclude--with some caveats--that SNAREs are indeed important in defining the specificity of vesicle targeting. SNAREs contain structural features called alpha -helices or coils. During membrane fusion, four alpha -helices from SNAREs found on the vesicle and target membranes come together to form a stable, four-helix bundle or coiled-coil. The formation of SNARE complexes is essential for membrane fusion, so a tremendous amount of research has been dedicated to understanding how these complexes form, and what they do.
ISSN:0028-0836
1476-4687
DOI:10.1038/35025176