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Mannstadt, M.

Publications and source records attributed to Mannstadt, M..

2 recordsLinked to original sources

TGF-β signaling regulates the response of the skeleton to phosphate

Inorganic phosphate (Pi) homeostasis is crucial to organismal health, yet the mechanisms underlying the regulation of it remain unclear. Critically, we lack a clear understanding of the Pi response circuitry in osteogenic cells that identifies altered serum Pi levels and transmits this information to changes in serum FGF23 levels, a key hormone regulating circulating Pi. We utilized genome-wide CRISPR screens in osteogenic Pi-responsive fluorescent reporter cell lines to identify regulators of the response to high phosphate, intersecting those results with loci associated with circulating FGF23 levels by genome-wide association studies (GWAS) and identified a potential role for TGF-{beta}2. We found that each of the three ligands (TGF-{beta}1, 2, 3) can enhance the response to Pi in osteogenic cell lines and ex vivo cultures of calvariae, while inhibitors of TGF{beta} receptor signaling dampen it. Co-treatment of Pi with TGF{beta} ligands led to an elevated, synergistic transcriptional induction of Slc20a1, which encodes a key Pi importer, which corresponded with an increased intracellular uptake of phosphate. Furthermore, in mice, blocking TGF{beta} signaling disrupted the induction of FGF23 in mice on a high phosphate diet, resulting in disrupted downstream endocrine control of phosphate homeostasis. Together, these findings reveal a role for TGF{beta} signaling in the regulation of phosphate homeostasis in osteogenic cells through regulation of cellular phosphate uptake, which in turn contributes to the maintenance of organismal phosphate homeostasis.

molecular biology↗

Phosphate dysregulation via the XPR1:KIDINS220 protein complex is a therapeutic vulnerability in ovarian cancer

Clinical outcomes for patients with ovarian and uterine cancers have not improved greatly in the past twenty years. To identify ovarian and uterine cancer vulnerabilities, we analyzed genome-scale CRISPR/ Cas9 loss-of-function screens across 739 human cancer cell lines. We found that many ovarian cancer cell lines overexpress the phosphate importer SLC34A2, which renders them sensitive to loss of the phosphate exporter XPR1. We extensively validated the XPR1 vulnerability in cancer cell lines and found that the XPR1 dependency was retained in vivo. Overexpression of SLC34A2 is frequently observed in tumor samples and is regulated by PAX8 -a transcription factor required for ovarian cancer survival. XPR1 overexpression and copy number amplifications are also frequently observed. Mechanistically, SLC34A2 overexpression and impaired phosphate efflux leads to the accumulation of intracellular phosphate and cell death. We further show that proper localization and phosphate efflux by XPR1 requires a novel binding partner, KIDINS220. Loss of either XPR1 or KIDINS220 results in acidic vacuolar structures which precede cell death. These data point to the XPR1:KIDINS220 complex - and phosphate dysregulation more broadly -as a therapeutic vulnerability in ovarian cancer.

cancer biology↗