Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Heindel U,Schmidt MF,Veit Mdoi
10.1016/s0014-5793(03)00449-6keywords:
subject
Has Abstractpub_date
2003-06-05 00:00:00pages
57-62issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579303004496journal_volume
544pub_type
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