   3.4.11.3 | S-acylation |
insulin-responsive aminopeptidase (IRAP) is identified as an S-acylated protein in adipocytes and other tissues, semi-quantitative acyl-RAC technique shows that approximately 60% of IRAP is S-acylated in 3T3-L1 adipocytes, palmitoylation. Mapping of the sites of S-acylation on IRAP to two cysteine residues, one of which is predicted to lie in the cytoplasmic side of the single transmembrane domain and the other which is just upstream of this transmembrane domain, these cysteines, C103, and C114, may be modified in a mutually-exclusive manner. Although S-acylation regulates the intracellular trafficking of several transmembrane proteins, no effects of mutating the modified cysteines on the plasma membrane localisation of IRAP in transfected HEK-293T cells are detected, suggesting that S-acylation is not essential for the movement of IRAP through the secretory pathway |
755404 |
