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• W2014249275 abstract "The success of targeting kinases in cancer with small molecule inhibitors has been tempered by the emergence of drug-resistant kinase domain mutations. In patients with chronic myeloid leukemia treated with ABL inhibitors, BCR-ABL kinase domain mutations are the principal mechanism of relapse. Certain mutations are occasionally detected before treatment, suggesting increased fitness relative to wild-type p210 BCR-ABL. We evaluated the oncogenicity of eight kinase inhibitor-resistant BCR-ABL mutants and found a spectrum of potencies greater or less than p210. Although most fitness alterations correlate with changes in kinase activity, this is not the case with the T315I BCR-ABL mutation that confers clinical resistance to all currently approved ABL kinase inhibitors. Through global phosphoproteome analysis, we identified a unique phosphosubstrate signature associated with each drug-resistant allele, including a shift in phosphorylation of two tyrosines (Tyr 253 and Tyr 257 ) in the ATP binding loop (P-loop) of BCR-ABL when Thr 315 is Ile or Ala. Mutational analysis of these tyrosines in the context of Thr 315 mutations demonstrates that the identity of the gatekeeper residue impacts oncogenicity by altered P-loop phosphorylation. Therefore, mutations that confer clinical resistance to kinase inhibitors can substantially alter kinase function and confer novel biological properties that may impact disease progression." @default.
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• W2014249275 date "2006-12-19" @default.
• W2014249275 modified "2023-09-27" @default.
• W2014249275 title "Phosphorylation of the ATP-binding loop directs oncogenicity of drug-resistant BCR-ABL mutants" @default.
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• W2014249275 doi "https://doi.org/10.1073/pnas.0609239103" @default.
• W2014249275 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1698443" @default.
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• W2014249275 hasPublicationYear "2006" @default.
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