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Numb/Numbl-Opo antagonism controls retinal epithelium morphogenesis by regulating integrin endocytosis

Ozren Bogdanović1, Mariana Delfino-Machín, María Nicolás-Pérez

  • 1Centro Andaluz de Biología del Desarrollo (CSIC/UPO/JA), 41013 Sevilla, Spain.

Developmental Cell
|October 9, 2012
PubMed

Insights

The transmembrane protein Opo regulates integrin endocytosis by interacting with Numb/Numbl. This process is crucial for polarized integrin localization and the basal constriction that shapes the vertebrate retina during development.

Area of Science:

  • Cell Biology
  • Developmental Biology
  • Molecular Biology

Background:

  • Polarized trafficking of adhesion receptors, like integrins, is critical for cell migration and tissue morphogenesis.
  • Clathrin-dependent endocytosis of integrins is essential for cell migration, but its role in epithelial tissue morphogenesis is less understood.

Purpose of the Study:

  • To investigate the role of the transmembrane protein Opo in epithelial tissue morphogenesis, specifically focusing on integrin trafficking.
  • To elucidate the mechanism by which Opo regulates integrin endocytosis and its impact on cellular behavior.

Main Methods:

  • Investigated the interaction between Opo, Numb, and Numbl using in vivo models.
  • Utilized gain-of-function experiments in teleost embryos to study the effects of altered Numb/Numbl activity.
  • Analyzed retinal malformations in opo mutants and compared them to experimental manipulations.

Main Results:

  • Opo antagonizes the function of clathrin adaptors Numb and Numbl through an integrin-like NPxF motif interaction.
  • Opo acts as a negative regulator of integrin endocytosis in vivo.
  • Gain-of-function of Numb/Numbl in teleost embryos recapitulates the retinal malformations observed in opo mutants.

Conclusions:

  • Developmental regulator Opo enables polarized integrin localization by modulating Numb/Numbl activity.
  • This modulation of integrin trafficking by Opo directs basal constriction, a key process in shaping the vertebrate retina epithelium.

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