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Di Feo, F.

Publications and source records attributed to Di Feo, F..

2 recordsLinked to original sources

Subthreshold perturbation of DNA replication induces a secretory response and a bystander effect in naïve human fibroblasts

Replication stress is a hallmark of cancer, where it drives DNA damage and genome instability. Yet subtle, subthreshold perturbations of DNA synthesis likely occur routinely in normal proliferating tissues, and their consequences for cell homeostasis are unknown. Using primary human fibroblasts, we show that doses of the DNA polymerase inhibitor aphidicolin, too low to engage the replication checkpoint, or produce detectable DNA breaks, nonetheless elicit low-level, ATM-dependent {gamma}H2AX phosphorylation uncoupled from overt damage. This near-silent perturbation reprograms gene expression, inducing replication-associated genes together with a discrete secretory programme dominated by matrix-remodelling proteases and matricellular factors. This output is not a senescence-associated secretory phenotype: the NF-{kappa}B/IL-1/IL-6 axis is co-ordinately repressed rather than induced, p53 target genes including CDKN1A are unchanged, and cells remain proliferative and non-senescent. Conditioned medium from exposed cells reproduces ATM-{gamma}H2AX activation in naive fibroblasts without DNA damage, defining a "perturbed-replication bystander effect" (PeRBE). PeRBE is ROS-independent and mediated by heat-labile, proteinaceous factors, and in recipient cells it induces an extracellular-matrix programme that culminates in increased collagen production, without loss of proliferative capacity. A perturbation invisible to every standard replication-stress assay therefore generates a transmissible, protein-borne signal that instructs fibrogenic matrix remodelling in cells that never experienced it.

cell biology↗

PHOSPHORYLATION-DEPENDENT ASSOCIATION OF WRN WITH RPA IS REQUIRED FOR RECOVERY OF REPLICATION FORKS STALLED AT SECONDARY DNA STRUCTURES

The WRN protein mutated in the hereditary premature aging disorder Werner syndrome plays a vital role in handling, processing, and restoring perturbed replication forks. One of its most abundant partners, Replication Protein A (RPA), has been shown to robustly enhance WRN helicase activity in specific cases when tested in vitro. However, the significance of RPA-binding to WRN at replication forks in vivo has remained largely unexplored. In this study, we have identified several conserved phosphorylation sites in the acidic domain of WRN that are targeted by Casein Kinase 2 (CK2). Surprisingly, these phosphorylation sites are essential for the interaction between WRN and RPA, both in vitro and in human cells. By characterizing a CK2-unphosphorylatable WRN mutant that lacks the ability to bind RPA, we have determined that the WRN-RPA complex plays a critical role in fork recovery after replication stress whereas the WRN-RPA interaction is not necessary for the processing of replication forks or preventing DNA damage when forks stall or collapse. When WRN fails to bind RPA, fork recovery is impaired, leading to the accumulation of single-stranded DNA gaps in the parental strands, which are further enlarged by the structure-specific nuclease MRE11. Notably, RPA-binding by WRN and its helicase activity are crucial for countering the persistence of G4 structures after fork stalling. Therefore, our findings reveal for the first time a novel role for the WRN-RPA interaction to facilitate fork restart, thereby minimizing G4 accumulation at single-stranded DNA gaps and suppressing accumulation of unreplicated regions that may lead to MUS81-dependent double-strand breaks requiring efficient repair by RAD51 to prevent excessive DNA damage.

cell biology↗