ABSTRACT
Famesyltransferase, a membrane-associated protein, catalyzes the addition of the 15-carbon fragment of famesyl diphosphate to the cysteine SH group of the CAAX motif containing protein substrates to regulate the function of target proteins through famesylation. As one of the most important target proteins of FTase, oncogenic forms of Ras mutants have been reportedly involved in more than 30% human cancers, and are known to play critical roles in cancer development and progression. Despite decades of research, Ras inhibitors are so elusive that no therapeutic agents directly targeting Ras mutants have been clinically approved, the primary reason for which is the lack of druggable pockets on the surface of Ras. Therefore, FTase, the main regulator of Ras protein, has gradually become a research hotspot, and many FTase inhibitors have been developed, synthesized and used for the treatment of malignant tumors. In the present review, we briefly describe the regulation of Ras functions by FTase and the role of FTase in cancers, and mainly explore the research progress of FTase inhibitors as a promising strategy for cancer therapy.