Fachbereich Veterinärmedizin


Service-Navigation

    Publikationsdatenbank

    Palmitoylation sites and processing of synaptotagmin I, the putative calcium sensor for neurosecretion (2003)

    Art
    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Autoren
    Heindel, Ulrich
    Schmidt, Michael F G
    Veit, Michael
    Quelle
    FEBS letters; 544(1/3) — S. 57–62
    ISSN: 0014-5793
    Sprache
    Englisch
    Verweise
    Pubmed: 12782290
    Kontakt
    Institut für Immunologie und Molekularbiologie

    Robert-von-Ostertag-Str. 7-13
    Gebäude 35
    14163 Berlin
    Tel.+49 30 838 - 518 34 Fax.+49 30 838 451 834

    Abstract / Zusammenfassung

    Synaptotagmin I, the calcium sensor for neurotransmission, is palmitoylated. We have identified the palmitoylation sites as five cysteine residues located between the transmembrane and cytoplasmic regions. In contrast to wild-type synaptotagmin, the non-acylated mutant is not converted to the endoglycosidase-H-resistant form after expression in CV-1 cells. This indicates a block in transport through the Golgi complex. However, when expressed in PC-12 and RBL cells non-acylated synaptotagmin is targeted to the plasma membrane and to secretory granules. No significant cleavage of [(3)H]palmitate from synaptotagmin was observed in pulse-chase experiments. This indicates that the majority of fatty acids are structural rather than dynamic components.