The selective deamination of adenosines (A) to inosines (I) in messenger RNAs (mRNAs) can alter the encoded protein's amino acid sequence, with often critical consequences on protein stability, localization, and/or function. Insulin-like growth factor-binding protein 7 (IGFBP7) supports cell-adhesion and stimulates fibroblast proliferation with IGF and insulin. It exists in both proteolytically processed and unprocessed forms with altered cell-extracellular matrix interactions. Here we show that editing of IGFBP7 transcripts impacts the protein's susceptibility to proteolytic cleavage, thus providing a means for a cell to modulate its functionality through A-to-I RNA editing.
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