spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online August 29, 2005
doi: 10.1242/10.1242/jcs.02561


Journal of Cell Science 118, 3819-3828 (2005)
Published by The Company of Biologists 2005
This Article
Right arrow Summary Freely available
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ungermann, C.
Right arrow Articles by Langosch, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ungermann, C.
Right arrow Articles by Langosch, D.

Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing

Christian Ungermann1 and Dieter Langosch2

1 Biochemie Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany
2 Lehrstuhl der Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354 Freising, Germany



View larger version (29K):

[in a new window]
 
Fig. 1. SNARE function in trafficking and SNARE domain structure. (A) Vesicle trafficking. The stages of vesicle budding and fusion are shown. During SNARE activation, SNAREs become disassembled with the help of NSF, {alpha}-SNAP and ATP. Budding includes uptake of the v-SNARE, Rab proteins and tethers, which assemble before or during tethering into a complete complex. Fusion requires SNARE complex assembly and lipid mixing. (B) Domain structure of selected SNAREs. Lipid anchors on Ykt6 and SNAP-25 are indicated. (C) The HABC N-terminal domain of syntaxin (PDB accession number 1BR0) (Fernandez et al., 1998Go). (D) The Ykt6 N-terminal longin domain (1H8M) (Tochio et al., 2001Go).

 


View larger version (38K):

[in a new window]
 
Fig. 2. SNARE complex assembly and its control. (A) Interaction of syntaxin with nSec1, also known as Munc18 (1DN1) (Yang et al., 2000Go). nSec1 binds to the closed conformation of syntaxin, regulating its availability. (B) Binding of Sly1 to the N-terminal peptide of the SNARE Sed5 may function similarly (1MQS) (Bracher and Weissenhorn, 2002Go). (C) The open conformation of the syntaxin molecule (as shown in Fig. 1C). (D) The assembled SNARE complex modeled between two membranes (1SFC) (Sutton et al., 1998Go). (E) Interaction of complexin with the SNARE complex might regulate exocytosis (1KIL) (Chen et al., 2002Go).

 


View larger version (20K):

[in a new window]
 
Fig. 3. Membrane fusion. (A) Putative model of SNARE-mediated membrane fusion. At stage I, Q- and R-SNAREs are separate from each other and the Q-SNARE syntaxin exists in its closed conformation. SNARE complex formation releases the Q-SNARE HABC N-terminal domain and is associated with vesicle docking (stage II). Several SNARE complexes may associate at the fusion site via their TMSs. Docking may result in hemifusion (III), which is followed by formation of lipidic (IV) or proteinaceous (V) fusion pores prior to full fusion (V). Note that proteins and membranes are not drawn to scale. (B) Lipid topology in hemifusion.

 





© The Company of Biologists Ltd 2005