Changing partners (original) (raw)

Membrane fusion

Nature volume 404, pages 347–348 (2000)Cite this article

Fusion of the membranes that surround cells and their intracellular organelles occurs during a variety of cellular processes. During neurotransmission, for example, neurons release chemical neurotransmitters from intracellular, membrane-bounded containers (vesicles) into the extracellular space, the synapse. This process involves the merging of the vesicle membrane and the presynaptic plasma membrane, allowing the neurotransmitter to be released. Yet before one membrane can merge with another, a series of protein interactions is required in a process that resembles changing partners at a square dance. On page 355 of this issue1, Misura and colleagues offer new insight into the relationship between two of these partners.

Central to the mechanism of membrane fusion are the SNAREs, which are proteins, found on the target membrane and on the vesicle, that catalyse membrane fusion by assembling into a complex that pins the two fusing membranes together. A key step in the assembly of the SNARE complex is the activation of syntaxin, a name that encompasses a family of SNARE proteins found on target membranes (the presynaptic plasma membrane in the case of neurotrans- mission). Thanks to the resolution of the three-dimensional structure of the core of a SNARE complex2, our understanding of membrane fusion is advancing apace to an atomic level; however, the mechanism by which syntaxin is activated remains poorly understood.

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Figure 1: A simplified model for membrane fusion, showing SNARE-complex assembly and conformational changes in syntaxin.

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Authors and Affiliations

  1. Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, PO Box 208002, New Haven, 06520-8002, Connecticut , USA
    Chavela M. Carr & Peter J. Novick

Authors

  1. Chavela M. Carr
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  2. Peter J. Novick
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Correspondence toPeter J. Novick.

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Carr, C., Novick, P. Changing partners.Nature 404, 347–348 (2000). https://doi.org/10.1038/35006200

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