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Vol. 16, Issue 4, 1811-1822, April 2005
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* Cell Biology Laboratory, Department of Biochemistry, BioSciences Institute, National University of Ireland, Cork, Ireland;
Division of Rheumatology and Immunology, Brigham and Women's Hospital, Boston, MA 02115
Submitted December 10, 2004;
Accepted January 11, 2005
Monitoring Editor: Carl-Henrik Heldin
By comparing differential gene expression in the insulin-like growth factor (IGF)-IR null cell fibroblast cell line (R– cells) with cells overexpressing the IGF-IR (R+ cells), we identified the Mystique gene expressed as alternatively spliced variants. The human homologue of Mystique is located on chromosome 8p21.2 and encodes a PDZ LIM domain protein (PDLIM2). GFP-Mystique was colocalized at cytoskeleton focal contacts with 
-actinin and 
1-integrin. Only one isoform of endogenous human Mystique protein, Mystique 2, was detected in cell lines. Mystique 2 was more abundant in nontransformed MCF10A breast epithelial cells than in MCF-7 breast carcinoma cells and was induced by IGF-I and cell adhesion. Overexpression of Mystique 2 in MCF-7 cells suppressed colony formation in soft agarose and enhanced cell adhesion to collagen and fibronectin. Point mutation of either the PDZ or LIM domain was sufficient to reverse suppression of colony formation, but mutation of the PDZ domain alone was sufficient to abolish enhanced adhesion. Knockdown of Mystique 2 with small interfering RNA abrogated both adhesion and migration in MCF10A and MCF-7 cells. The data indicate that Mystique is an IGF-IR–regulated adapter protein located at the actin cytoskeleton that is necessary for the migratory capacity of epithelial cells.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: Rosemary O'Connor (r.oconnor{at}ucc.ie).
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