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

Bandzählung: 544

Heftzählung: 1/3

Seiten: 57 – 62

ISSN: 0014-5793

Sprache

Englisch

Verweise

Pubmed: 12782290

Kontakt

Institut für Immunologie

Robert-von-Ostertag-Str. 7-13
14163 Berlin
+49 30 838 51834
immunologie@vetmed.fu-berlin.de

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.