Literature DB >> 8455717

SNAP receptors implicated in vesicle targeting and fusion.

T Söllner1, S W Whiteheart, M Brunner, H Erdjument-Bromage, S Geromanos, P Tempst, J E Rothman.   

Abstract

The N-ethylmaleimide-sensitive fusion protein (NSF) and the soluble NSF attachment proteins (SNAPs) appear to be essential components of the intracellular membrane fusion apparatus. An affinity purification procedure based on the natural binding of these proteins to their targets was used to isolate SNAP receptors (SNAREs) from bovine brain. Remarkably, the four principal proteins isolated were all proteins associated with the synapse, with one type located in the synaptic vesicle and another in the plasma membrane, suggesting a simple mechanism for vesicle docking. The existence of numerous SNARE-related proteins, each apparently specific for a single kind of vesicle or target membrane, indicates that NSF and SNAPs may be universal components of a vesicle fusion apparatus common to both constitutive and regulated fusion (including neurotransmitter release), in which the SNAREs may help to ensure vesicle-to-target specificity.

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Year:  1993        PMID: 8455717     DOI: 10.1038/362318a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  968 in total

1.  Early requirement for alpha-SNAP and NSF in the secretory cascade in chromaffin cells.

Authors:  T Xu; U Ashery; R D Burgoyne; E Neher
Journal:  EMBO J       Date:  1999-06-15       Impact factor: 11.598

Review 2.  Neurosecretory cells without neurosecretion: evidence of an independently regulated trait of the cell phenotype.

Authors:  M L Malosio; R Benfante; G Racchetti; B Borgonovo; P Rosa; J Meldolesi
Journal:  J Physiol       Date:  1999-10-01       Impact factor: 5.182

3.  Selective formation of Sed5p-containing SNARE complexes is mediated by combinatorial binding interactions.

Authors:  M M Tsui; W C Tai; D K Banfield
Journal:  Mol Biol Cell       Date:  2001-03       Impact factor: 4.138

4.  TRAPP stably associates with the Golgi and is required for vesicle docking.

Authors:  J Barrowman; M Sacher; S Ferro-Novick
Journal:  EMBO J       Date:  2000-03-01       Impact factor: 11.598

5.  A new class of fusion-associated small transmembrane (FAST) proteins encoded by the non-enveloped fusogenic reoviruses.

Authors:  M Shmulevitz; R Duncan
Journal:  EMBO J       Date:  2000-03-01       Impact factor: 11.598

6.  Resolution of patch capacitance recordings and of fusion pore conductances in small vesicles.

Authors:  K Debus; M Lindau
Journal:  Biophys J       Date:  2000-06       Impact factor: 4.033

7.  Fusion between retinal rod outer segment membranes and model membranes: functional assays and role for peripherin/rds.

Authors:  K Boesze-Battaglia
Journal:  Methods Enzymol       Date:  2000       Impact factor: 1.600

8.  The role of the tethering proteins p115 and GM130 in transport through the Golgi apparatus in vivo.

Authors:  J Seemann; E J Jokitalo; G Warren
Journal:  Mol Biol Cell       Date:  2000-02       Impact factor: 4.138

9.  Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs.

Authors:  W Nickel; T Weber; J A McNew; F Parlati; T H Söllner; J E Rothman
Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-26       Impact factor: 11.205

10.  Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain.

Authors:  F Parlati; T Weber; J A McNew; B Westermann; T H Söllner; J E Rothman
Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-26       Impact factor: 11.205

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