Supracellular contractility in Xenopus laevis embryonic epithelia regulated by extracellular nucleotides and the purinergic G-protein coupled receptor P2Y2

Sagar D. Joshi, Timothy R. Jackson, Lin Zhang, Carsen Stuckenholz, Lance A. Davidson
2025 · doi:10.1101/2025.01.21.634176
preprint OA: closed CC-BY-NC-ND-4.0
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This paper investigates how extracellular nucleotides regulate supracellular contractility in Xenopus laevis embryonic epithelia, building on prior findings that wounded embryo lysate can trigger transient epithelial contraction. Using temporal/spatial activity screens, inhibitor testing, and morpholino knockdown of candidate receptors, the authors find that extracellular ADP, UTP, and UDP can induce contractility, with ATP and UTP being major contributors from the lysate. They show that this response is mediated by the purinergic GPCR P2Y2 (P2RY2), which via G-protein signaling promotes F-actin assembly and myosin II contractility, and that P2RY2 knockdown (or mutant G-protein overexpression) abrogates contraction when epithelia are exposed to eATP or lysate. The study is limited to Xenopus embryonic epithelia and does not directly assess human disease contexts. The paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

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Abstract Extracellular signals regulate epithelial homeostasis, cell fate and pattern cell behaviors during embryogenesis, wound healing, regeneration, and disease progression. Previous studies in our group found cell lysate from intentionally wounded embryos triggers a strong but transient contraction in neighboring epithelia, whether contiguous to the wound site or in non-wounded embryos. We previously identified extracellular ATP (eATP) as a possible candidate. Here we test additional candidates and find several nucleotides including ADP, UTP, and UDP also trigger contractility. Through a temporal and spatial screen of lysate activity, an inhibitor screen, and morpholino knock-down of candidate receptors, we find contractility is mediated by a G-protein coupled purinergic receptor P2Y2 (P2RY2). Activated P2RY2 triggers F-actin assembly and myosin II contractility. Knockdown of P2RY2 or overexpression of mutant G-protein effectors abrogate epithelial contractility when epithelia are exposed to eATP or lysate. We demonstrate that the major contributors to epithelial contractility in lysate are extracellular nucleotide triphosphates ATP and UTP, which are sensed by P2RY2 and transduced through G-proteins to contract the epithelium. Summary Statement Contractility of the Xenopus embryonic epithelium can be driven by extracellular nucleotides ATP or UTP and actuated by the G-protein coupled purinergic receptor P2Y2 (P2RY2). Highlights Extracellular nucleotides ATP and UTP can trigger epithelial contractility. Epithelia contract in response to (ATP ∼ UTP) > (ADP ∼ UDP) > ADO (adenosine). The purinergic G-protein coupled receptor P2Y2 is responsible for this contractile response by indirectly modulating actomyosin contractility. Competing Interest Statement The authors have declared no competing interest. Footnotes Updated reagent in methods and added acknowledgements.

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