Sin1, a regulatory subunit of TOR protein kinase, has an evolutionarily conserved domain that specifically binds and recruits substrate for phosphorylation, and may represent a potential target for anti-cancer drugs.

Despite BCAAs being de novo-synthesized in chloroplasts, TOR activation by BCAAs is conserved in plants and triggers a re-organization of actin and actin-associated endomembranes.

Atg9 inhibits TOR signaling to regulate cell growth and tissue homeostasis in Drosophila adult midgut.

Young defense metabolites are often believed to be solely outputs but evidence suggests that they can regulate ancient signaling pathways.

The Rag-family GTPases, known activators of TOR complex 1 (TORC1), also function as attenuator that prevents deregulated hyperactivation of TORC1 signaling.

TOR kinase guides the transition of plant stem cells from the dormant embryonic state to the active adult state by integrating light and metabolic signals.

Plants and humans use a shared mechanism, the eukaryotic metabolic sensor TARGET OF RAPAMYCIN protein kinase and its substrate, an RNA-binding protein called LARP1, to coordinate post-transcriptional gene expression.

A domain called the 'Conserved region in the middle' is responsible for target recognition in the TORC2 complex in fission yeast and the mTORC2 complex in mammals.