We’ve recently shown that p210 BCR ABL TK precludes JNK and 14 3 3 sigma phosphorylation in reaction to DNA damage thus keeping p145 h ABL in-active bound to 14 3 3 sigma within the cytoplasm. Accordingly, inhibition of the fusion protein enzymatic activity by IM promotes JNK activating nuclear transfer, 14 3 3 sigma phosphorylation, AG-1478 clinical trial p145 d ABL launch and phosphorylation. Here, we noted the secondary effects of IM and mTOR inhibitor RAD001 on p145 c ABL service and sub cellular re-location in CML cells. RAD001 can be an ester derivative of the macrolide antifungal antibiotic rapamycin. I-t forms acomplex with-the peptidyl prolyl cis trans isomerase FKBP12 which binds to the FRB domain located in the N terminal mTOR kinase domain thereby resulting in mTOR inhibition. RAD001 owns built-in anti proliferative and pro apoptotic activity on BCR ABL indicating cells proceeding in the prolonged inhibition of mTOR initiating phosphorylation at Ser2448 and the following dissociation ofmTORC1 components. As expected, mTOR inhibition in a reaction to RAD001 induced JNK initiating phosphorylation at Thr183 selling, in turn, the phosphorylation of 14 3 3 sigma at Ser184, the pre-requisite for p145 c ABL launch. However, despite JNK induced phosphorylation of 14 3 3 sigma RAD001 alone left p145 d ABL limited to the cytoplasm either free or bound to 14 3 3 sigma. The Skin infection event is probably conditional upon RAD001 minor effect on 14 3 3 sigma term and its lacking effects on p145 c ABL phosphorylation at serine containing residues associated with 14 3 3 recognition, two additional elements contributing to p145 cABL nuclear import in reaction to IM. JNK and 14 3 3 sigma phosphorylation were improved by persistent mTOR inactivation in response to RAD001 either alone or in connection with IM. Probably improved JNK and 14 3 3 sigma phosphorylation did not play a vital role in improved of nuclear accumulation p145 c Celecoxib solubility ABL in response to IM and RAD001 organization, as they are triggered by IM alone as well as other events responsible for p145 c ABL nuclear translocation, including 14 3 3 sigma reduction and p145 c ABL p phosphorylation at serinecontaining motifs mixed up in recognition and binding to 14 3 3. In case of p145 c ABL it depends on two different phosphoserinecontaining motifs and by phosphorylation at Thr735, a residue included inside the 14 3 3 binding motif RSXpS/TXP that likely masks the nuclear localization signals inside the c ABL protein C terminal domain. Thr735 phosphorylation status is not associated with p145 c ABL dissociation from 1-4 3 3 in response to oxidative stress and IM, but seems crucial for p145 c ABL cytoplasmatic localization under unstressed circumstances and nuclear export following genotoxic stress.