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© The Rockefeller University Press, 0021-9525/2000//1063 $5.00
The Journal of Cell Biology, Volume 149, Number 5, , 2000 1063-1072

Original Article

Snarepins Are Functionally Resistant to Disruption by Nsf and {alpha}SNAP



Thomas Webera, Francesco Parlatia, James A. McNewa, Robert J. Johnstona, Benedikt Westermanna, Thomas H. Söllnera, and James E. Rothmana

a Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Ave., New York, NY 10021.(212) 717-3604(212) 639-8598

j-rothman{at}ski.mskcc.org

SNARE (SNAP [soluble NSF {N-ethylmaleimide–sensitive fusion protein} attachment protein] receptor) proteins are required for many fusion processes, and recent studies of isolated SNARE proteins reveal that they are inherently capable of fusing lipid bilayers. Cis-SNARE complexes (formed when vesicle SNAREs [v-SNAREs] and target membrane SNAREs [t-SNAREs] combine in the same membrane) are disrupted by the action of the abundant cytoplasmic ATPase NSF, which is necessary to maintain a supply of uncombined v- and t-SNAREs for fusion in cells. Fusion is mediated by these same SNARE proteins, forming trans-SNARE complexes between membranes. This raises an important question: why doesn't NSF disrupt these SNARE complexes as well, preventing fusion from occurring at all? Here, we report several lines of evidence that demonstrate 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. This elegant design allows fusion to proceed locally in the face of an overall environment that massively favors SNARE disruption.

Key Words: membrane fusion • SNARE • NSF • {alpha}SNAP • liposomes

© 2000 The Rockefeller University Press

Thomas Weber's present address is Institute for Gene Therapy and Molecular Medicine, Box 1496, Mount Sinai School of Medicine, 1425 Madison Ave., New York, NY 10029-6574.

Benedikt Westermann's present address is Institute for Physiological Chemistry, Ludwig-Maximilians University Munich, Goethestrasse 33, 80336 Munich, Germany.

Abbreviations used in this paper: BoNT D, botulinum neurotoxin D; NSF, N-ethylmaleimide–sensitive fusion protein; SNAP, soluble NSF attachment protein; SNAP-25, synaptosome-associated protein of 25 kD; SNARE, SNAP receptor; t-SNARE, target membrane SNARE; VAMP, vesicle-associated membrane protein; v-SNARE, vesicle SNARE.


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