Growth is a fundamental property of cells and is regulated in response to nutritional/environmental conditions a cell is experiencing. This regulation comes from signaling pathways that cells possess. TOR, an essential eukaryotic kinase, through TORC1 and TORC2 regulates cellular/organismal growth homeostasis. In S. cerevisiae, TORC2 is anchored at plasma membrane in MCTs. Increase in PM tension causes Slm1 to relocate from eisosomes to MCTs to activate TORC2. However, mechanism of how Slm1 activate TORC2 remains unknown. We identified that Slm1 BAR and PH domains are sufficient to perform its functions. We show that Slm1 BAR domain contributes to PI(4,5)P2 binding indirectly through dimerization which brings two PI(4,5)P2 binding PH domains in close vicinity. We showed that Slm1 oligomerizes via it's BAR domain that remodels membranes. We show that oligomerization together with PI(4,5)P2 binding are essential for Slm1 to activate TORC2. We provide a biochemical reconstitution of Slm1 mediated TORC2 activation.