![]() ![]() Structures and complexes of TOR kinase in eukaryotes Among these findings, the identification of target of rapamycin (TOR) was a landmark discovery. Nonetheless, its mechanism of action remained largely unknown for approximately 20 years until several breakthrough findings were published, including identifying this molecule's in vivo protein targets in yeast and mammalian cells in the early 1990s ( Heitman et al., 1991 Koltin et al., 1991 Lane et al., 1991 Michnick et al., 1991 Cafferkey et al., 1993 Kunz et al., 1993 Brown et al., 1994 Chiu et al., 1994 Sabatini et al., 1994 Sabers et al., 1995). Subsequent studies of rapamycin revealed its amazing antifungal, immunosuppressive, and anticancer properties ( Martel et al., 1977 Houchens et al., 1983 Eng et al., 1984). This compound was then named “rapamycin” in reference to its place of origin ( Sehgal et al., 1975 Vezina et al., 1975) ( Figure 1A). In 1975, Sehgal and colleagues purified a macrolide compound from the bacterial species, Steptomyces hygroscopicus, which was isolated from a soil sample collected on Rapa Nui (Easter Island). ![]() Finally, we summarize the impact of dysregulation of TOR signaling on every stage of plant growth and development, from embryogenesis and seedling growth, to flowering and senescence. ![]() We present an overview of plant TOR complexes, analyze the signaling landscape of the plant TOR signaling network from the upstream signals that regulate plant TOR activation to the downstream effectors involved in various biological processes, and compare their conservation and specificities within different biological contexts. Here, we review recent discoveries on the plant TOR signaling network. ![]() During evolution, TOR both maintains the highly conserved TOR complex compositions, and cellular and molecular functions, but also evolves distinctive roles and strategies to modulate cell growth, proliferation, metabolism, survival, and stress responses in eukaryotes. Target of rapamycin (TOR) is an evolutionarily conserved protein kinase that functions as a central signaling hub to integrate diverse internal and external cues to precisely orchestrate cellular and organismal physiology. ![]()
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