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

FEBS Letters

Veit, Michael¹  Heindel, Ulrich¹  Schmidt, Michael F.G¹ 

[1] Department of Immunology and Molecular Biology, Veterinary-Medical Faculty, Free University Berlin, Philippstraße 13, 10115 Berlin, Germany

关键词: Neurosecretion;    Synaptotagmin;    Synaptosomal 25 kDa protein;    Palmitoylation;    Glycosylation;    Intracellular transport;    SNARE;    SNAP receptor;    SNAP-25;    synaptosomal protein with a molecular weight of 25 kDa;    NGF;    nerve growth factor;    Endo-H;    endoglycosidase-H;   

DOI  :  10.1016/S0014-5793(03)00449-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 [³H]palmitate from synaptotagmin was observed in pulse-chase experiments. This indicates that the majority of fatty acids are structural rather than dynamic components.

【 授权许可】

Unknown