The target of rapamycin complex 1 (TORC1) is a central kinase that coordinates 
nutrient availability with eukaryotic cell growth. Although TORC1 signaling is 
repressed by various stresses in yeast, the underlying mechanisms remain 
elusive. Here we report that TORC1 signaling upon heat stress is regulated by 
stress granules (SGs), which are cytoplasmic foci formed under certain stresses. 
Ectopic formation of SGs achieved by Pbp1 overexpression in unstressed cells 
sequesters TORC1 in this compartment, thereby blunting TORC1 signaling. Upon 
heat stress, a physiological SG-inducing condition, TORC1 is also recruited to 
SGs, which delays reactivation of TORC1 signaling during recovery from heat 
stress. Moreover, TORC1 reactivation is directed through SG disassembly, 
suggesting that SGs act as a key determinant for TORC1 reactivation during 
recovery from heat stress. Furthermore, this mechanism contributes to reduction 
of heat-induced mutations. Thus, TORC1 signaling is coupled to heat-induced SGs 
to protect cells from DNA damage.