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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

View larger version (20K): [in a new window]   Fig. 1. Three-dimensional representation of the ß-barrel structures of human mIL-1 (Graves et al., 1990) and human FGF1 (Lozano et al., 2000). ß-sheet domains are indicated in yellow and are depicted as rotating counter clockwise around the open centers of the structures. The structures were downloaded from the Protein Data Bank of the NCBI (http://www.rcsb.org/pdb/).

View larger version (38K): [in a new window]   Fig. 2. Models of FGF1 (above) and IL-1 (below) stress-induced release pathways. I, Actin cytoskeleton-dependent transport of the release complex components. II, Cu2+-dependent formation of the release complex at the inner leaflet of the cell membrane. III, Association of the release complex with annexin II. IV, Phosphatidylserine-dependent flipping of the release complex through the cell membrane.