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Vol. 9, Issue 3, 585-597, March 1998
Department of Cell Biology and Physiology, Washington University
School of Medicine, St. Louis, Missouri 63110
Synaptosomal-associated protein of 25 kDa (SNAP-25) is a
palmitoylated membrane protein essential for neurotransmitter release from synaptic terminals. We used neuronal cell lines to study the
biosynthesis and posttranslational processing of SNAP-25 to investigate
how palmitoylation contributes to the subcellular localization of the
protein. SNAP-25 was synthesized as a soluble protein that underwent
palmitoylation approximately 20 min after synthesis. Palmitoylation of
the protein coincided with its stable membrane association. Treatment
of cells with brefeldin A or other disrupters of transport inhibited
palmitoylation of newly synthesized SNAP-25 and abolished membrane
association. These results demonstrate that the processing of SNAP-25
and its targeting to the plasma membrane depend on an intact transport
mechanism along the exocytic pathway. The kinetics of SNAP-25
palmitoylation and membrane association and the sensitivity of these
parameters to brefeldin A suggest a novel trafficking pathway for
targeting proteins to the plasma membrane. In vitro, SNAP-25 stably
associated with membranes was not released from the membrane after
chemical deacylation. We propose that palmitoylation of SNAP-25 is
required for initial membrane targeting of the protein but that other
interactions can maintain membrane association in the absence of fatty
acylation.
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