Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25.
Synaptotagmin, a likely calcium sensor for synaptic transmission, and SNAP-25, a t-SNARE of the presynaptic plasma membrane, are key proteins for the docking and fusion of synaptic and other vesicles. We report that both synaptotagmin and SNAP-25 are palmitoylated with their fatty acids attached in a labile thioester-type bond. A SNAP-25 mutant with deleted palmitoylation sites is found exclusively in the cytosol after cell fractionation, whereas the palmitoylated form of SNAP-25 is membrane-bound, establishing that SNAP-25 is membrane-anchored via covalently linked palmitate.
Veit
M
M
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, 10021, USA.
Söllner
T H
TH
Rothman
J E
JE
D000215:Acylation; D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins; D002458:Cell Fractionation; D002462:Cell Membrane / Q000737:chemistry; D003545:Cysteine / Q000737:chemistry; D003600:Cytosol / Q000737:chemistry; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000032:analysis / Q000737:chemistry*; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000737:chemistry*; D050765:Qa-SNARE Proteins; D050825:Synaptosomal-Associated Protein 25; D050857:Synaptotagmins
D002135:Calcium-Binding Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D010169:Palmitic Acids; D050765:Qa-SNARE Proteins; D050825:Synaptosomal-Associated Protein 25; D050857:Synaptotagmins; D019308:Palmitic Acid; D003545:Cysteine