Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 8 August 2006
Vol. 2006, Issue 347, p. tw273
[DOI: 10.1126/stke.3472006tw273]

EDITORS' CHOICE

CELL BIOLOGY Understanding SNARE-Mediated Membrane Fusion

Cellular membrane fusion involves the formation of a four-helix bundle with contributions from vesicle and target membrane SNARE (soluble NSF attachment protein receptor) proteins. SNAREs constitute the minimal fusion machinery and can promote the fusion of liposomes. Pobbati et al. dissected the SNARE assembly process in greater detail. In vitro experiments with liposomes showed that SNARE assembly was initiated at the N-terminal region of the four-helix bundle and that was sufficient to drive rapid liposome fusion. Giraudo et al. used a system in which SNARE proteins, which are normally expressed on intracellular membranes, are "flipped" so that they are exposed at the cell surface. Cells expressing such flipped SNARES fuse spontaneously. By introducing a fusion clamp (complexin) and a calcium sensor (synaptotagmin), cell-cell fusion can be regulated by calcium in a comparable way to the regulation seen during neurotransmitter release.

A. V. Pobbati, A. Stein, D. Fasshauer, N- to C-terminal SNARE complex assembly promotes rapid membrane fusion. Science 313, 673-676 (2006). [Abstract] [Full Text]

C. G. Giraudo, W. S. Eng, T. J. Melia, J. E. Rothman, A clamping mechanism involved in SNARE-dependent exocytosis. Science 313, 676-680 (2006). [Abstract] [Full Text]

Citation: Understanding SNARE-Mediated Membrane Fusion. Sci. STKE 2006, tw273 (2006).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882