TOR is a protein kinase that was first identified as the molecular target of rapamycin in yeast by Heitman and colleagues in 1991 (Heitman et al., 1991), while the mammalian TOR homolog was discovered independently by several groups just 3 years later (Sabitini et al., 1994; Erdjument-Bromage et al., 1994; Chiu et al., 1994; Brown et al., 1994; Chen et al., 1995). Rapamycin is a macrolide compound that was first discovered in the 1970s as an anti-fungal agent. It was thus initially considered as an antibiotic (Vezina et al., 1975; Singh et al., 1979; Sehgal et al., 1975; Baker et al., 1978). Tor is the central component of two biochemically and functionally distinct multiprotein compleses (TORC1 and 2, Figs. 1 and 2) that play crucial roles within cells by coordinating diverse signals - including nutrient availability and hormones - with the control of a range of physiological and pathophysiological cell processes. mTORC1 and mTORC2 are controlled by different signals.
|Title of host publication||Encyclopedia of Biological Chemistry|
|Place of Publication||Netherlands|
|Number of pages||17|
|Publication status||Published - 29 Jul 2021|