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Papers In Press, published online ahead of print April 19, 2001
Department of Biochemistry, Kansas State University, Manhattan, KS 66053
Corresponding Author: zolkiea{at}ksu.edu
ADAM 12, a member of the ADAM family of transmembrane metalloprotease-disintegrins, has been previously implicated in differentiation of skeletal myoblasts. In the present study, we show that the cytoplasmic tail of mouse ADAM 12 interacts in vitro and in vivo with the SH3 domain of the p85
J. Biol. Chem, 10.1074/jbc.M101162200
Submitted on February 6, 2001
Revised on April 19, 2001
Accepted on April 18, 2001
Direct interaction between the cytoplasmic tail of ADAM 12 and the SH3 domain of p85alpha activates phosphatidylinositol 3-kinase in C2C12 cells
regulatory subunit of phosphatidylinositol (PI) 3-kinase. By site-directed mutagenesis, we have identified three p85 binding sites in ADAM 12 involving PXXP motifs located at amino acids 825-828, 833-836, and 884-887. Using green fluorescent protein (GFP)-pleckstrin homology (PH) domain fusion protein as a probe for PI 3-kinase lipid products, we have further demonstrated that expression of ADAM 12 in C2C12 cells resulted in translocation of GFP-PH to the plasma membrane. This suggests that transmembrane ADAM 12, by providing docking sites for the SH3 domain of p85, activates PI 3-kinase by mediating its recruitment to the membrane. Since PI 3-kinase is critical for terminal differentiation of myoblasts, and since expression of ADAM 12 is up-regulated at the onset of the differentiation process, ADAM 12-mediated activation may constitute one of the regulatory mechanisms for PI 3-kinase during myoblast differentiation.
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