Model demonstrating how the PAG complex contributes to T-cell anergy. Enhanced PAG-phosphorylation by Fyn leads to increased recruitment and activity of Csk. This results in enhanced phosphorylation of Y⁵²⁹ within Fyn, which, together with the phosphorylation of Y²¹⁵, further enhances Fyn kinase activity. This facilitates the phosphodependent recruitment of RasGAP onto PAG within the rafts, where it stimulates the intrinsic GTPase activity of Ras, thereby preventing the translocation of active Ras out of the rafts. Secondly, increased Sam68 binding may stabilize the complex and free mRNAs for anergy-inducing factors; also, increased Sam68 expression can block cyclin D1, thus preventing the G₁/S transition.