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Simonet, J. C.

Publications and source records attributed to Simonet, J. C..

2 recordsLinked to original sources

Starve-Feed Cycles Direct Quiescence to Proliferation Transitions in Drosophila Follicle Stem Cells via Transcriptional Regulation

Stem cell quiescence is a reversible state in which cells temporarily exit the cell cycle but remain poised to reenter, on cue. Robust protection of the balance between stem cell quiescence and proliferation (Q->P) is critical for long-term tissue health. Proliferation without proper resources drives disease states including cancer or birth defects. Conversely, extended periods of quiescence can lead to irreversible senescence, causing stem cell loss, aging symptoms, and vulnerability to oncogenic transformation. Diet is a central regulator of Q->P. Tissue stem cells are particularly impacted, entering periods of quiescence during nutrient restriction, with rapid induction of proliferation upon feeding. We demonstrated previously that the Hedgehog (Hh) signaling pathway is necessary and sufficient for controlling Q->P responses to dietary changes in epithelial Follicle Stem Cells (FSCs) in the fly ovary. The Hh effector, Cubitus Interruptus (Ci), is a transcriptional regulator that mediates the feeding response. To identify Ci-induced Q->P regulators, we labeled transcripts that are induced in FSCs during the 6-hour Q->P timecourse using thiouracil tagging (TU-tagging), and sequenced TU-tagged messages versus Input to prioritize candidates. Unexpectedly, cell cycle regulators were not induced, suggesting that other mechanisms control Q->P in FSCs. We describe a sequential screening approach that uncovered seven novel, feeding-dependent Q->P regulators, including a cholesterol transporter and, surprisingly, glial and neuronal regulators. Our results highlight the importance of dynamic regulation of gene expression for translation of dietary signals by stem cells, uncovering new pathways for mechanistic investigation.

genetics↗

IMPDH1 retinal variants control filament architecture to tune allosteric regulation

IMP dehydrogenase (IMPDH), a key regulatory enzyme in purine nucleotide biosynthesis, dynamically assembles filaments in response to changes in metabolic demand. Humans have two isoforms: IMPDH2 filaments reduce sensitivity to feedback inhibition by the downstream product GTP, while IMPDH1 assembly remains uncharacterized. IMPDH1 plays a unique role in retinal metabolism, and point mutants cause blindness and disrupt GTP regulation. Here, in a series of cryo-EM structures we show that IMPDH1 assembles polymorphic filaments with different assembly interfaces in active and inhibited states. Retina-specific splice variants introduce structural elements that reduce sensitivity to GTP inhibition, including stabilization of the active filament form. Finally, we show that IMPDH1 disease mutations fall into two classes: one disrupts GTP regulation and the other has no in vitro phenotype. These findings provide a foundation for understanding the role of IMPDH1 in retinal function and disease and demonstrate the diverse mechanisms by which metabolic enzyme filaments are allosterically regulated.

biochemistry↗