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• W2153387139 abstract "Significance Echinoderm microtubule-associated protein (EMAP)-like (EML) proteins normally function in the cytoskeleton. In some lung cancers, genetic abnormalities generate the oncogenic fusion protein EML4-anaplastic lymphoma kinase (ALK) on which the cancer cells depend for survival. We have determined the molecular structure of a conserved, tubulin-binding region of EML1 that reveals an unexpected protein fold. This region is disrupted in ∼70% of EML4-ALK fusions found in patients, causing them to be sensitive to drugs that target Hsp90, a cellular factor that stabilizes misfolded protein. Our findings will potentially enable more effective, stratified therapy of EML4-ALK nonsmall cell lung cancer and suggest that the truncation of a globular domain at the translocation breakpoint may prove generally predictive of Hsp90 inhibitor sensitivity in cancers driven by fusion oncogenes." @default.
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• W2153387139 date "2014-03-24" @default.
• W2153387139 modified "2023-10-14" @default.
• W2153387139 title "Crystal structure of EML1 reveals the basis for Hsp90 dependence of oncogenic EML4-ALK by disruption of an atypical β-propeller domain" @default.
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• W2153387139 doi "https://doi.org/10.1073/pnas.1322892111" @default.
• W2153387139 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3986153" @default.
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