Regulates cell growth, chemotaxis, signal relay and the actin cytoskeleton. Required for chemoattractant receptor and G protein-mediated activation of the 12 transmembrane domain adenylyl cyclase. Functions as a part of protein complex TORC2. TORC2, is presumed to be indirectly negatively modulated by rapamycin and regulates actin polarization. TORC2, but not TORC1, negatively regulates phagocytosis. This protein and dagA protein CRAC, a cytosolic regulator, are both essential for activation of the enzyme adenylyl cyclase. This protein and CRAC do not function redundantly. Both proteins are integral components of the adenylyl cyclase activation pathway. Part of a complex, TORC2, consisting of tor, lst8, piaA and ripA. Additional proteins, such as 14-3-3 and heat-shock proteins, may also belong to the TORC2 complex. Expression peaks between 2.5 and 5 hours of development. Cells are unable to aggregate on bacterial lawns and show impaired chemotaxis, rounded morphology and lack polarity. Phosphorylations of endogenous pkbA/PKB substrates greatly reduced including loss of phosphorylation at 'Thr-470' in endogenous pkgB. In null cells neither chemoattractant stimulation of intact cells nor guanosine gamma thio-phosphate treatment of lysates activates the enzyme adenylyl cyclase. Constitutive expression of piaA reverses these defects. dagA and piaA double mutants require both proteins for reconstitution and activation of adenylyl cyclase. Null cells can respond to exogenous signals by expression of developmental genes necessary for spore formation, although the efficiency of the process is reduced. Null cells possess the machinery to respond to cAMP signals. However, they are unable to aggregate in pure populations suggesting that the defect may be in the production of the cAMP signals. Belongs to the RICTOR family.