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Highlights • Identification of a structurally novel inhibitor of the UNC119-Src interaction • Impairment of UNC119-medicated Src plasma membrane enrichment • Reduction of activating Src Y416 autophosphorylation • Reduction of growth and clonogenic potential of Src-dependent cells Summary Interference with the signaling activity of the N-myristoylated nonreceptor protein tyrosine kinase Src is considered a viable approach in anti-cancer drug discovery.
In order to compare the localisations of polybasic-stretch-containing Src and dually palmitoylated Fyn, both SFKs were C-terminally fused to mCitrine (Src-mCit and Fyn-mCit) and expressed in HeLa cells. These recombinant proteins preserved the regulation of their autocatalytic activity and were expressed at approximately equal or lower levels as compared to endogenous SFKs (Supplementary Fig. 1).
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