ArticlePlacenta2021
PLAC1 affects cell to cell communication by interacting with the desmosome complex.
Article in Placenta, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Transcriptomic Analysis ofInternational journal of molecular sciences · 2026Article
- Transcriptomic Analysis ofbioRxiv : the preprint server for biology · 2026Article
- Fundamental and unique roles of PLAC1 in the regulation of rat and human trophoblast cell development.Development (Cambridge, England) · 2026Article
- Plac1Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A genome-wide shRNA screen uncovers a novel potential ligand for NK cell activating receptors.Frontiers in immunology · 2025Article
- Changes in plasma PLAC-1 concentration and its expression during early-mid pregnancy in bovine placental tissues - a pilot study.BMC veterinary research · 2024Article
- Desmoglein-2 as a cancer modulator: friend or foe?Frontiers in oncology · 2023Review
- Identifying driver modules based on multi-omics biological networks in prostate cancer.IET systems biology · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
introductionX-linked PLAC1 is highly expressed in placenta during embryogenesis, and when ablated in mice, causes aberrant placental cell layer organization. It is also highly expressed in many types of cancer cell-lines. Although it has been shown that it promotes AKT phosphorylation in cancer cells, the exact mechanism by which it influences placental layer differentiation is unclear.
methodsTo investigate the mechanism of action of PLAC1 we did cell fractionation and immunoprecipitation of the protein and Mass Spectrometry analysis to identify its interaction partners. The associated proteins were directly tested for interactions by co-transfection with PLAC1 and immunoprecipitation. Mutations in the ZP-N domain of PLAC1 were introduced to assess its involvement in the interactions.
resultsWe provide evidence that Desmoglein-2 (DSG2), a component of the membrane-associated desmosomal complex, directly interacts with PLAC1. Mutations of cysteines in ZP-N domain disrupt the interaction between PLAC1 and DSG-2. DISCUSSION: Because desmosomes are responsible for establishing lateral cell-cell junctions, we suggest that direct interaction with the lateral junction protein complex may be implicated in the PLAC1 effects on cell-cell interactions, and thereby on the layer structure of the placenta.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.