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Originally published In Press as doi:10.1074/jbc.M102925200 on May 10, 2001

J. Biol. Chem., Vol. 276, Issue 27, 25549-25557, July 6, 2001
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Copper Induces the Assembly of a Multiprotein Aggregate Implicated in the Release of Fibroblast Growth Factor 1 in Response to Stress*

Matteo LandriscinaDagger , Cinzia Bagalá, Anna Mandinova, Raffaella Soldi, Isabella Micucci§, Stephen Bellum, Igor Prudovsky, and Thomas Maciag

From the Center for Molecular Medicine, Maine Medical Center Research Institute, Scarborough, Maine 04074 and the Center for the Biophysical Sciences, University of Maine, Orono, Maine 04469

Fibroblast growth factor (FGF) 1 is known to be released in response to stress conditions as a component of a multiprotein aggregate containing the p40 extravescicular domain of p65 synaptotagmin (Syt) 1 and S100A13. Since FGF1 is a Cu2+-binding protein and Cu2+ is known to induce its dimerization, we evaluated the capacity of recombinant FGF1, p40 Syt1, and S100A13 to interact in a cell-free system and the role of Cu2+ in this interaction. We report that FGF1, p40 Syt1, and S100A13 are able to bind Cu2+ with similar affinity and to interact in the presence of Cu2+ to form a multiprotein aggregate which is resistant to low concentrations of SDS and sensitive to reducing conditions and ultracentrifugation. The formation of this aggregate in the presence of Cu2+ is dependent on the presence of S100A13 and is mediated by cysteine-independent interactions between S100A13 and either FGF1 or p40 Syt1. Interestingly, S100A13 is also able to interact in the presence of Cu2+ with Cys-free FGF1 and this observation may account for the ability of S100A13 to export Cys-free FGF1 in response to stress. Lastly, tetrathiomolybdate, a Cu2+ chelator, significantly represses in a dose-dependent manner the heat shock-induced release of FGF1 and S100A13. These data suggest that S100A13 may be involved in the assembly of the multiprotein aggregate required for the release of FGF1 and that Cu2+ oxidation may be an essential post-translational intracellular modifier of this process.

* This work was supported in part by National Institutes of Health Grants HL32348 and AG98503 (to T. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported in part by a fellowship from the Catholic University of Rome, Italy.

§ Present address: Dept. of Geriatric Medicine, University of Florence, School of Medicine, Florence, Italy.

To whom correspondence should be addressed: Center for Molecular Medicine, Maine Medical Center Research Inst., 81 Research Dr., Scarborough, ME 04074. Tel.: 207-885-8200; Fax: 207-885-8179; E-mail: maciat@mmc.org.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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