A synaptic vesicle protein with a novel cytoplasmic domain and four transmembrane regions
TC Südhof, F Lottspeich, P Greengard, E Mehl, R Jahn - Science, 1987 - science.org
TC Südhof, F Lottspeich, P Greengard, E Mehl, R Jahn
Science, 1987•science.orgComplementary DNA and genomic clones were isolated and sequenced corresponding to
rat and human synaptophysin (p38), a major integral membrane protein of synaptic vesicles.
The deduced amino acid sequences indicate an evolutionarily highly conserved protein that
spans the membrane four times. Both amino and carboxyl termini face the cytoplasm, with
the latter containing ten copies of a tyrosine-rich pentapeptide repeat. The structure of
synaptophysin suggests that the protein may function as a channel in the synaptic vesicle …
rat and human synaptophysin (p38), a major integral membrane protein of synaptic vesicles.
The deduced amino acid sequences indicate an evolutionarily highly conserved protein that
spans the membrane four times. Both amino and carboxyl termini face the cytoplasm, with
the latter containing ten copies of a tyrosine-rich pentapeptide repeat. The structure of
synaptophysin suggests that the protein may function as a channel in the synaptic vesicle …
Complementary DNA and genomic clones were isolated and sequenced corresponding to rat and human synaptophysin (p38), a major integral membrane protein of synaptic vesicles. The deduced amino acid sequences indicate an evolutionarily highly conserved protein that spans the membrane four times. Both amino and carboxyl termini face the cytoplasm, with the latter containing ten copies of a tyrosine-rich pentapeptide repeat. The structure of synaptophysin suggests that the protein may function as a channel in the synaptic vesicle membrane, with the carboxyl terminus serving as a binding site for cellular factors.
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