PARP-7 is a mono(ADP-ribosyl) transferase that directs an extensive ADP-ribosylated proteome to control microtubule stability, and regulate ovarian cancer cell growth and motility.

A combined chemical genetics, proximity labeling, and ADP-ribose site mapping approach shows that PARP-7 mono-ADP-ribosylates immune-relevant proteins on cysteine amino acids.

Formation and cell pole-localization of chemotactic signaling-arrays is a coupled process mediated by ParP, which drives localized array-assembly and regulates the localization-dynamics of its network constituents.

Using a cross-species phenotypic drug discovery pipeline, compounds promoting rod photoreceptor survival in zebrafish and mouse models of retinitis pigmentosa were identified, evidence of additive effects of paired compounds and inhibition of PARP-dependent cell death suggest novel therapeutic strategies.

In C. elegans and mouse neurons, the balance between poly(ADP-ribose) glycohydrolases and poly(ADP-ribose) polymerases regulates axon regeneration downstream of DLK-1/MAPKKK signaling.

MicroRNAs tightly control the cellular level of homologous recombination (HR) factors in the G1 phase, and failure of this control system results in an ectopic increase in HR proteins in G1 cells leading to impaired DNA repair.

Transgenic mice and cell models provide evidence of a pathophysiological mechanism that connects mtDNA damage to cardiac dysfunction via reduced NAD⁺ levels and loss of mitochondrial function and communication.

Upon genotoxic stress, the FBXL10-RNF68-RNF2 ubiquitin ligase complex mono-ubiquitylates histone H2A and mediates H2A/H2A.Z exchange to repress transcription and ensures proper high fidelity homologous recombination repair.

Biochemical approaches and cellular experiments show a novel effect of METTL3 on homologous recombination repair and chemotherapeutic response via the m6A-YTHDC1-dependent regulation of the EGF/RAD51 axis.