Fibroblast growth factor 9 secretion is mediated by a non-cleaved amino-terminal signal sequence.
Journal of Biological Chemistry. 2000-03-01; 275(11): 8083-8090
DOI: 10.1074/jbc.275.11.8083
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Revest JM(1), DeMoerlooze L, Dickson C.
Author information:
(1)Imperial Cancer Research Fund, 44 Lincoln’s Inn Fields, London WC2A 3PX,
United Kingdom.
Fibroblast growth factors are a family of intercellular signaling molecules with
multiple and varied roles in animal development. Most are exported from cells by
means of a classical amino-terminal signal sequence that is cleaved from the
mature protein during its passage through the secretory pathway. Fibroblast
growth factor-9 (Fgf-9) does not contain a recognizable signal sequence,
although it is efficiently secreted. In this study, we show that Fgf-9 enters
the endoplasmic reticulum and traverses the Golgi complex in a similar manner to
other constitutively secreted proteins. Deletion and point mutation analysis has
revealed an atypical non-cleaved signal sequence within the amino-terminal
region of Fgf-9. Moreover, the first 28 amino acids of Fgf-9 can function as an
efficient non-cleaved signal peptide when appended to the amino terminus of
green fluorescent protein.
DOI: 10.1074/jbc.275.11.8083
PMID: 10713129 [Indexed for MEDLINE]