TY - JOUR
T1 - SNAP family of NSF attachment proteins includes a brain-specific isoform
AU - Whiteheart, Sidney W.
AU - Griff, Irene C.
AU - Brunner, Michael
AU - Clary, Douglas O.
AU - Mayer, Thomas
AU - Buhrow, Susan A.
AU - Rothman, James E.
PY - 1993
Y1 - 1993
N2 - 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.
AB - 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.
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U2 - 10.1038/362353a0
DO - 10.1038/362353a0
M3 - Article
C2 - 8455721
AN - SCOPUS:0027402091
SN - 0028-0836
VL - 362
SP - 353
EP - 355
JO - Nature
JF - Nature
IS - 6418
ER -