Search bioRxiv⌕ Search

bioRxiv · 10.1101/2025.10.14.682359

Prolactin receptor localization and dynamics: Insights from quantitative imaging and mathematical modeling

Abstract

Signal transduction through the prolactin receptor (PRLR) is crucial in pancreatic {beta}-cell pro-liferation, impacting pancreatic homeostasis. PRLR-induced JAK/STAT signaling is dynamic, involving changes in spatial organization of signaling molecules. Thus, the spatial organization of PRLR could have strong implications on signaling output. Internalization has been shown and modeled in other signaling pathways but has not been considered in a mathematical model of PRLR signaling. Here, we use live-cell fluorescence imaging, reconstitution approaches, and fluorescence correlation spectroscopy (FCS) to inform a mathematical model of PRLR signaling. Internal PRLR localization is observed in primary pancreatic tissue and in an engineered PRLR expression system. Our imaging data indicate the presence of intracellular and plasma membrane-bound receptor populations. We use FCS to resolve the membrane-bound PRLR population. Based on our data, we include internalization dynamics within an ordinary differential equation (ODE) model of PRLR signaling. We employ the model to explore how the spatial heterogeneity of PRLR affects downstream signaling. We show that the model is more sensitive to PRLR trafficking rates and ability to promote signaling than to its initial spatial distribution. Our data underscore the versatility of a modeling-imaging framework to quantitatively understand signal transduction in and beyond {beta}-cells. Significance StatementO_LIProlactin receptor (PRLR) signal transduction impacts the growth and survival of insulin-secreting cells, making this pathway a target for building our understanding of pancreatic homeostasis and exploring potential diabetes therapeutics. C_LIO_LILive fluorescence imaging techniques applied within an engineered PRLR expression platform indicate PRLR localization patterns consistent with primary pancreatic tissue and the presence of two spatially distinct PRLR populations. These observations inform a predictive mathematical model of PRLR signaling. C_LIO_LIIntegrating experimental data tailored to computational approaches shapes our understanding of complex, multiscale systems such as signal transduction. A generalizable modeling-imaging framework enables the study of molecular dynamics beyond {beta}-cells. C_LI

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Cherchia, L., Fraser, S. E., Finley, S. D., Schneider, F.. 2025-10-14. Prolactin receptor localization and dynamics: Insights from quantitative imaging and mathematical modeling. https://doi.org/10.1101/2025.10.14.682359

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Sequence context and partner availability specify divergent cell fates from a single transcription factor

Transcription factors drive the gene regulatory networks that control developmental transitions, yet which of their many targets a cell uses remains unresolved. Expressing Cebp, Cebp{beta} or Cebp{delta} identically, alone or with Oct4, Sox2, Klf4 and cMyc, gave four outcomes: adipocyte from fibroblasts and neural stem cells, trophectoderm from embryonic stem cells, and myeloid from B cells. Raising Cebp levels changed how many sites it reached, not which sequence it read: clustered motifs maintained somatic enhancers, while spillover onto low-copy sites created de novo enhancers carrying composites of Cebp and cell-type-restricted partners. In fibroblasts, Cebp also redistributed Oct4, Sox2 and Klf4 from early targets, blocking iPSC formation. Supplying the predicted partners rewrote the output: Spi1 redirected Cebp into parallel adipogenic and myeloid programs, via a transient PpargCD45 state using separate enhancers for each; TFAP2C abolished adipogenic conversion. Motif density and partner composites therefore assemble a factor's instructive output in the receiving cell.

cell biology↗

Tracking the conformational dynamics of single molecules in live cells; GTPase cycling in Cdc42 gradients and microclusters

The Rho family of GTPases play a critical role in many cellular processes by acting as molecular switches relying on conformational changes to transition between active and inactive states. The spatial distribution and kinetics of these conformational changes are complex and vary across the cell. We describe here biosensors based on environment-responsive fluorescent dyes, capable of reporting the conformational changes of individual GTPase molecules as they traffic within living cells (SPARC Cdc42 and SPARC Rac1, 'Single Particle Activation Reporter Constructs'). We use SPARC Cdc42 to determine the rates of different steps in GTPase regulation, activation/inactivation and membrane insertion, that together generate localized gradients of Cdc42 activity driving cell motility. The biosensors also revealed heterogeneously distributed clusters of Cdc42, the mechanisms of their activation, and potential roles in polarized motility.

cell biology↗

High-content screening identifies FDA-approved activators of mitophagy

Mitochondrial diseases are highly heterogeneous disorders caused by defects in oxidative phosphorylation, for which only limited therapeutic options are available. The elimination of dysfunctional mitochondria via mitophagy activation is an attractive strategy to treat several mitochondrial diseases, irrespective of the underlying genetic defect. To identify pharmacological activators of this pathway, we performed a high-content screening of 1,971 FDA-approved compounds using cellular reporters of TFEB nuclear translocation and mitophagy. This screening identified 294 compounds that promoted TFEB translocation, nine of which increased the number of mitolysosomes without compromising cell viability or damaging mitochondria. Among the selected compounds, Meptazinol and Ponatinib emerged as the top-ranked mitophagy inducers in fibroblasts from patients with complex I and IV deficiency, respectively, and were prioritised for further characterisation. However, they did not rescue the bioenergetic defect, suggesting that the stimulation of mitophagy per se is not sufficient to ameliorate the OXPHOS defect in mitochondrial diseases. Overall, our findings establish a scalable platform for the identification of pharmacological activators of TFEB and identify candidate compounds for therapeutic modulation of mitophagy.

cell biology↗