Abstract: |
THE soluble NSF attachment proteins (SNAPs) enable N-ethyl-maleimide- sensitive fusion protein (NSF) to bind to target mem-branes1-4. Here we report the cloning and sequencing of com-plementary DNAs encoding α-, β- and γ-SNAPs. Two of these proteins, α and γ, are found in a wide range of tissues, and act synergistically in intra-Golgi transport. The third, β, is a brain-specific isoform of α-SNAP. Thus, NSF and SNAPs appear to be general components of the intracellular membrane fusion apparatus, and their action at specific sites of fusion must be controlled by SNAP receptors particular to the membranes being fused, as described in the accompanying article4. © 1993 Nature Publishing Group. |
Keywords: |
unclassified drug; nonhuman; animal; mice; animal tissue; animalia; molecular cloning; cloning, molecular; amino acid sequence; molecular sequence data; hybrid protein; carrier proteins; recombinant proteins; organ specificity; base sequence; dna sequence; cattle; protein family; blotting, northern; brain protein; tissue specificity; intracellular membranes; membrane fusion; brain chemistry; bos taurus; female; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; n ethylmaleimide; nsf attachment protein; n ethylmaleimide sensitive membrane fusion protein
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