Fibroblast Growth Factor 9 Secretion Is Mediated by a Non-cleaved Amino-terminal Signal Sequence

• Published in: The Journal of biological chemistry Vol. 275; no. 11; pp. 8083 - 8090
• Main Authors: Revest, Jean-Michel, DeMoerlooze, Laurence, Dickson, Clive
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 17.03.2000; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Animals; Biological Assay; Biological Transport; Cell Compartmentation; Endoplasmic Reticulum; Endoplasmic Reticulum - metabolism; Fibroblast Growth Factor 9; Fibroblast Growth Factors; Glycosylation; Golgi Apparatus; Golgi Apparatus - metabolism; Growth Substances; Growth Substances - genetics; Growth Substances - metabolism; Growth Substances - pharmacology; Life Sciences; Mice; Molecular Sequence Data; Protein Processing, Post-Translational; Protein Sorting Signals; Recombinant Fusion Proteins; Recombinant Fusion Proteins - metabolism; Sequence Deletion
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.275.11.8083

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.