Synaphin: A protein associated with the docking/fusion complex in presynaptic terminals

Toru Ishizuka, Hideo Saisu, Shoji Odani, Teruo Abe

    Research output: Contribution to journalArticlepeer-review

    74 Citations (Scopus)

    Abstract

    We previously identified a 19 kDa protein associated with the docking/fusion complex involved in neurotransmitter release. A cDNA for this protein was cloned from a bovine brain cDNA library using an oligonucleotide probe based on its partial amino acid sequence. The protein (named synaphin) en coded by the cDNA is a very hydrophilic protein rich in glutamic acid and lysine residues. It lacks any putative transmembrane segments or strongly hydrophobic domains. Immunoblots with antibodies against synaphin detected the protein only in the nervous system among the tissues examined In brain, it exists mainly in the soluble fraction and is scarce in synaptic vesicles.

    Original languageEnglish
    Pages (from-to)1107-1114
    Number of pages8
    JournalBiochemical and biophysical research communications
    Volume213
    Issue number3
    DOIs
    Publication statusPublished - 1995

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Fingerprint

    Dive into the research topics of 'Synaphin: A protein associated with the docking/fusion complex in presynaptic terminals'. Together they form a unique fingerprint.

    Cite this