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The alternative translation of synaptotagmin 1 mediates the non-classical release of FGF1.

Abstract：

:Although the extravesicular p40 domain of the transmembrane protein, p65 synaptotagmin (Syt) 1, is essential for the non-classical export of the signal peptide-less structure, FGF1, it was not possible to identify a specific intracellular protease responsible for the processing of p65 Syt1. Surprisingly, analysis of the p65 Syt1 coding sequence revealed the presence of two potential alternative ATG codons corresponding to Met103 and Met113 both of which were flanked by Kozak sequences. Indeed, in vitro translation of a Met103Ile but not a Met113Ile p65 Syt1 point mutant exhibited reduced expression of p40 Syt1 and the double p65 Syt1 Met103Ile and Met113Ile point mutant was unable to translate the p40 Syt1 isoform. Since the expression of the p65 Syt1 double point mutant inhibited the stress-induced release of FGF1, it is likely that the alternative translation of the p65 Syt1 transcript at Met103 may be involved in the generation of intracellular p40 Syt1, a critical component of the FGF1 release pathway.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Bagalá C,Kolev V,Mandinova A,Soldi R,Mouta C,Graziani I,Prudovsky I,Maciag T

doi

10.1016/j.bbrc.2003.09.119

subject

Has Abstract

pub_date

2003-10-31 00:00:00

pages

1041-7

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006291X03019107

journal_volume

310

pub_type

杂志文章

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