A targeting signal in VAMP regulating transport to synaptic vesicles.
VAMP is a synaptic vesicle membrane protein required for fusion. Synaptic vesicle targeting was measured for mutants of an epitope-tagged form of VAMP in transfected PC12 cells. A signal within a predicted amphipathic alpha helix is essential for targeting to synaptic vesicles. Cellubrevin, a nonneural VAMP homolog, contains this signal and is also targeted to synaptic vesicles. Amino acid substitutions within the synaptic vesicle targeting signal either enhance or inhibit sorting of VAMP to synaptic vesicles, but do not affect the ability of VAMP to form complexes with syntaxin and SNAP-25.
Grote
E
E
Department of Biochemistry and Biophysics, Hormone Research Institute, University of California, San Francisco 94143-0534, USA.
Hao
J C
JC
Bennett
M K
MK
Kelly
R B
RB
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001692:Biological Transport; D017124:Conserved Sequence; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016716:PC12 Cells; D010449:Peptide Mapping; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; D051381:Rats; D013572:Synaptic Vesicles / Q000502:physiology*
D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins