Complex regulation of RETINOBLASTOMA-RELATED's interactions with E2Fs via phosphorylation
Authors: Magyar, Z., Pettko-Szandtner, A., Vadai-Nagy, F., Gombos, M., Hlacs, A., Molnar, E., Marton, A., Vizler, C., Shiekh Bin Hamid, R., Kalo, P., Feher, A.
Category: Plant Biology
Model Organism: Arabidopsis thaliana
▶ AI Summary
The study maps CDK-mediated phosphorylation of Arabidopsis RBR, revealing that while many phosphorylated forms still bind E2Fs, multi‑phosphorylated RBR with a phosphorylated S911 site loses association with E2Fs and DREAM components and instead binds RNA‑binding proteins linked to ribosome biogenesis and translation. S911 phosphorylation is enriched in proliferating cells and rapidly declines after DNA damage, suggesting it switches RBR from a proliferation to a quiescence role, and molecular modeling indicates this site becomes inaccessible when RBR is complexed with E2Fs.