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Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
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PI3K-AKT, JAK2-STAT3 pathways and cell-cell contact regulate maspin subcellular localization.

M T Longhi1, L E Silva1, M Pereira1

  • 1Instituto de Ciencias Biomedicas, Departamento de Biologia Celular e do Desenvolvimento, Universidade de Sao Paulo, Av. Prof. Lineu Prestes, 1524, São Paulo, SP, 05508-000, Brazil.

Cell Communication and Signaling : CCS
|August 15, 2021
PubMed
Summary

Epidermal Growth Factor Receptor (EGFR) signaling, specifically via PI3K-Akt and JAK2-STAT3 pathways, influences maspin nuclear localization. Cell-cell contact also plays a critical role in regulating maspin

Keywords:
Cell-to-cell contactEGFRJAK2-STAT3MaspinPI3K-AkT

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Maspin (SERPINB5) is a tumor suppressor gene involved in cell growth, death, and adhesion.
  • Nuclear localization of maspin is crucial for its tumor suppressor activity.
  • EGFR activation promotes maspin nuclear localization in MCF-10A cells.

Purpose of the Study:

  • To identify EGFR downstream signaling molecules regulating maspin nuclear localization.
  • To investigate the influence of cell-cell contact on maspin nuclear localization.

Main Methods:

  • MCF-10A cells were treated with EGFR pathway inhibitors and EGF.
  • Maspin subcellular localization was assessed using immunofluorescence.
  • Proteomic and interactome analyses identified maspin-binding proteins.
  • Cell-cell contact effects were studied using chelating agents and varying cell densities.

Main Results:

  • PI3K-Akt and JAK2-STAT3 pathways, not MAPK, mediate EGF-induced maspin nuclear accumulation.
  • Maspin is nuclear in sparse cells but cytoplasmic in confluent cells, even with EGF.
  • Proteomics suggest maspin's role in post-transcriptional regulation, protein folding, and cell adhesion.

Conclusions:

  • Maspin nuclear accumulation is regulated by an interplay between EGFR signaling (PI3K-Akt, JAK2-STAT3) and cell-cell contact.
  • Cell-cell adhesion influences maspin's subcellular localization, impacting its function.