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First published online November 18, 2003
doi: 10.1242/10.1242/jcs.00872

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The non-classical export routes: FGF1 and IL-1 point the way

¹ Center for Molecular Medicine, Maine Medical Center Research Institute, 81 Research Drive, Scarborough, Maine 04074, USA
² Department of Oncology, Catholic University of Rome, School of Medicine, Rome 00168, Italy
³ Department of Geriatric Medicine, University of Florence, School of Medicine, Florence 50139, Italy

^* Author for correspondence (e-mail: maciat{at}mmc.org)

Non-classical protein release independent of the ER-Golgi pathway has been reported for an increasing number of proteins lacking an N-terminal signal sequence. The export of FGF1 and IL-1, two pro-angiogenic polypeptides, provides two such examples. In both cases, export is based on the Cu²⁺-dependent formation of multiprotein complexes containing the S100A13 protein and might involve translocation of the protein across the membrane as a `molten globule'. FGF1 and IL-1 are involved in pathological processes such as restenosis and tumor formation. Inhibition of their export by Cu²⁺ chelators is thus an effective strategy for treatment of several diseases.

Key words: Fibroblast growth factor 1, FGF1, Interleukin 1, IL-1, Release, Non-classical, Copper, Synaptotagmin 1, S100A13

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