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The timing of peak prenylated Rap1 activation downstream of CDC42 or Rac is likely regulated by the endocytosis of CDC42 or the recycling of Rac to the plasma membrane as well as the cell-cycle-dependent availability of TCL cells ([@R5]). CDC42 and Rac1 endocytosis are Rho GTPase specific, as other Rho GTPases such as RhoA, Cdc42, and Rac1 lacking K-ras homology 2 (RH2) domain (e.g., Rnd2) have different prenylation requirement and fail to activate downstream effectors (fig. S5) ([@R26]). Specifically, as we found that GDP-locked CDC42 and Rac1 are inactivated in inactive T cells, it is likely that GTP-locked CDC42 and Rac1, which is unbound to guanine nucleotides, are rendered inactive after endocytosis. However, a previous study has shown that the GDP-locked CDC42 mutant (T17N) retained the ability to activate RalB ([@R22]), suggesting that the effector specificity could be determined by the level of GTP-binding affinity. This consideration is further strengthened by our finding that the cysteine-S-prenylation-mimicking mutant RhoA-C17 can still recruit the effector RalGDS, despite its impaired GTP-binding affinity (fig. S6).

We showed that the activation of the effectors, NF-κB and MAPK, is only dependent on prenylated CDC42 and Rac1 but not RhoA or Rnd2. The requirement of CDC42 and Rac1 prenylation on signaling differs from that of other endocytosis-related proteins, such as the Eps8-Rac1 interaction ([@R27]) or Eps15-Rac1 binding ([@R28], [@R29]). This is likely due to the fact that the S-

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