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

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 Lett

journal_title

FEBS letters

authors

Heindel U,Schmidt MF,Veit M

doi

10.1016/s0014-5793(03)00449-6

keywords:

subject

Has Abstract

pub_date

2003-06-05 00:00:00

pages

57-62

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579303004496

journal_volume

544

pub_type

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