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Comment
. 1999 Oct 26;96(22):12227-9.
doi: 10.1073/pnas.96.22.12227.

SNARE proteins mediate lipid bilayer fusion

J B Bock, R H Scheller
Comment

SNARE proteins mediate lipid bilayer fusion

J B Bock et al. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Figure 1
Figure 1
Historical hypothesized role of SNAREs in membrane trafficking. (A) The synaptic vesicle protein synaptotagmin was found to interact with the plasma membrane protein syntaxin, which also interacts with Ca++ channels. (B) Trans-SNARE complexes dock vesicles and provide a scaffold for the assembly of the fusion apparatus. (C) Parallel alignment of SNARES forces membranes into close apposition. (D) Current hypothesis that SNARE complex formation is regulated by proteins such as n-sec1. Membrane fusion occurs in concert with trans-SNARE complex formation. α-SNAP and NSF then break apart cis-SNARE complexes to reset the system for another round of fusion.
Figure 2
Figure 2
Localization of SNARE proteins within the secretory pathway of a typical eukaryotic cell. Members of the syntaxin family are colored red. SNAP-25 family members are green, and VAMP family members are blue. N, nucleus; ER, endoplasmic reticulum; SER, smooth ER; IC, intermediate compartment; TGN, trans-Golgi network; V, vesicles; DCV, dense core vesicles; EE, early endosome; LE, late endosome; L, lysosome; CV, clathrin-coated vesicles.
See this image and copyright information in PMC

Comment on

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