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Papers In Press, published online ahead of print March 3, 2003
Van Andel Research Institute, Grand Rapids, MI 49503
Corresponding Author: sara.courtneidge{at}vai.org
Fish is a scaffolding protein and Src substrate. It contains an amino terminal PX domain, five SH3 domains, as well as multiple motifs for binding both SH2 and SH3 domain-containing proteins. We have determined that the PX domain of Fish binds 3-phosphorylated phosphatidylinositols (including PtdIns3P and PtdIns(3,4)P2). Consistent with this, a fusion protein of green fluorescent protein (GFP) and the Fish PX domain localized to punctate structures similar to endosomes in normal fibroblasts. However, the full length Fish protein was largely cytoplasmic, suggesting that its PX domain may not be able to make intermolecular interactions in unstimulated cells. In Src-transformed cells, we observed a dramatic re-localization of some Fish molecules to actin-rich structures called podosomes: the PX domain was both necessary and sufficient to effect this translocation. We used a phage display screen with the fifth SH3 domain of Fish, and isolated ADAM19 as a binding partner. Subsequent analyses in mammalian cells demonstrated that Fish interacts with several members of the ADAMs family, including ADAMs 12, 15 and 19. In Src-transformed cells, ADAM12 co-localized with Fish in podosomes. Since members of the ADAMs family have been implicated in growth factor processing as well as cell adhesion and motility, Fish could be acting as an adaptor molecule that allows Src to impinge on these processes.
J. Biol. Chem, 10.1074/jbc.M300267200
Submitted on January 9, 2003
Revised on February 19, 2003
Accepted on March 3, 2003
The adaptor protein Fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells
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