IGFBP7's susceptibility to proteolysis is altered by A-to-I RNA editing of its transcript.

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.