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- W2944440933 abstract "Fibrolamellar carcinoma (FLC) is a rare liver cancer. FLCs uniquely produce DNAJ-PKAc, a chimeric enzyme consisting of a chaperonin-binding domain fused to the Cα subunit of protein kinase A. Biochemical analyses of clinical samples reveal that a unique property of this fusion enzyme is the ability to recruit heat shock protein 70 (Hsp70). This cellular chaperonin is frequently up-regulated in cancers. Gene-editing of mouse hepatocytes generated disease-relevant AML12DNAJ-PKAc cell lines. Further analyses indicate that the proto-oncogene A-kinase anchoring protein-Lbc is up-regulated in FLC and functions to cluster DNAJ-PKAc/Hsp70 sub-complexes with a RAF-MEK-ERK kinase module. Drug screening reveals Hsp70 and MEK inhibitor combinations that selectively block proliferation of AML12DNAJ-PKAc cells. Phosphoproteomic profiling demonstrates that DNAJ-PKAc biases the signaling landscape toward ERK activation and engages downstream kinase cascades. Thus, the oncogenic action of DNAJ-PKAc involves an acquired scaffolding function that permits recruitment of Hsp70 and mobilization of local ERK signaling." @default.
- W2944440933 created "2019-05-16" @default.
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- W2944440933 date "2019-05-07" @default.
- W2944440933 modified "2023-10-14" @default.
- W2944440933 title "An acquired scaffolding function of the DNAJ-PKAc fusion contributes to oncogenic signaling in fibrolamellar carcinoma" @default.
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- W2944440933 doi "https://doi.org/10.7554/elife.44187" @default.
- W2944440933 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6533061" @default.
- W2944440933 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31063128" @default.
- W2944440933 hasPublicationYear "2019" @default.
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