Search bioRxiv⌕ Search

Biology subjects

Premashankar, A.

Publications and source records attributed to Premashankar, A..

2 recordsLinked to original sources

Rewiring DNA repair with PARP-based chemical inducers of proximity

Chemical inducers of proximity (CIPs) can elicit durable--and often neomorphic--biological effects through the formation of a ternary complex, even at low equilibrium occupancy of their targets. This "event-driven" pharmacology is exemplified by CIPs that promote targeted protein degradation, but other applications remain underexplored. We developed a generalizable strategy to discover event-driven CIPs by tracking the cellular effects of heterobifunctional small molecules alongside quantitative measures of intracellular target engagement. Using this approach, we discovered PCIP-1, which inhibits DNA repair by recruiting BET proteins to PARP2. Unlike conventional PARP inhibitors, PCIP-1 activity is observed at low equilibrium occupancy of PARP1/2 and without inhibition of PARP-catalyzed PARylation, yet it retains synthetic lethality in cancer cells with homologous recombination deficiencies. PARP1 knockout, which confers resistance to conventional PARP drugs, increases sensitivity to PCIP-1, offering a potential new mechanism to overcome clinical resistance. Through these studies, we demonstrate that DNA repair can be rewired by CIPs and introduce a new form of event-driven pharmacology.

cancer biology↗

Phosphorylation-dependent mitotic SUMOylation drives nuclear envelope-chromatin interactions

In eukaryotes, chromatin binding to the inner nuclear membrane (INM) and nuclear pore complexes (NPCs) contributes to spatial organization of the genome and epigenetic programs important for gene expression. In mitosis, chromatin-nuclear envelope (NE) interactions are lost and then formed again as sister chromosomes segregate to post-mitotic nuclei. Investigating these processes in S. cerevisiae, we identified temporally and spatially controlled phosphorylation-dependent SUMOylation events that positively regulate post-metaphase chromatin association with the NE. Our work establishes a phosphorylation-mediated targeting mechanism of the SUMO ligase Siz2 to the INM during anaphase, where Siz2 binds to and SUMOylates the VAP protein Scs2. The recruitment of Siz2 through Scs2 is further responsible for a wave of SUMOylation along the INM that supports the assembly and anchorage of subtelomeric chromatin at the INM and localization of an active gene (INO1) to NPCs during the later stages of mitosis and into G1-phase.

cell biology↗