The epigenetic plasticity of a cell determines how malleable its chromatin landscape is. Developmental Pluripotency Associated 2 and 4 (DPPA2/4) are heterodimerising DNA-binding proteins that are restricted to the early embryo where they facilitate epigenetic plasticity1,2. Through analyses of several cancer datasets, we found that DPPA2/4 are re-expressed in a subset of cancers, in particular non-small cell lung cancer (NSCLC) where co-expression of DPPA2/4 signifies poorer outcomes. We hypothesised that re-expression of these developmental regulators may be promoting heightened embryonic-like plasticity in these cancers.
To understand the functional roles of DPPA2/4 in cancer, we depleted DPPA2 and/or DPPA4 by RNAi or CRISPR-KO in the NCI-H661 NSCLC cell line and performed molecular and phenotypic characterisations. Endogenous DPPA2/4 protein immunoprecipitation and mass spectrometry were used to identify bound cofactors. Through this we confirmed DPPA2/4 forms heterodimers, with stoichiometry revealing strong heterodimeric preferences for DPPA2 that we found to be necessary for protein stability. The DPPA2 interactors also included the H3K36me2 histone demethylase, KDM2A3. ChIP-seq revealed both DPPA2 and KDM2A were co-enriched at CpG rich genic regions. RNA-seq revealed that DPPA2/4 depletion had minimal effects on gene transcription which posits a model where DPPA2/4 prime the epigenome for future gene expression changes following selective pressure. Supporting this, initial ATAC-seq nucleosome position analysis showed that DPPA2 binds both open and closed chromatin, suggesting pioneer activity. Consistently, depletion of DPPA2/4 led to a loss of chromatin accessibility at gene promoters associated with chromatin organisation and DNA damage/repair. Supporting an epigenetic priming model, phenotypic assays demonstrated increased chemosensitivity and reduced cell viability, colony formation and cell migration upon DPPA2/4 depletion indicating their importance in driving cancer cell adaptation. Collectively we show that DPPA2/4 contribute to malignant phenotypes in NSCLC through their molecular functions as epigenetic priming factors.