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Amot and Yap1 regulate neuronal dendritic tree complexity and locomotor coordination in mice

Katarzyna O Rojek1, Joanna Krzemień1, Hubert Doleżyczek1

  • 1Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland.

Plos Biology
|May 3, 2019
PubMed

Insights

Angiomotin (Amot) and Yes-associated protein 1 (Yap1) are crucial for neuron development. These proteins regulate dendrite growth and brain structure, impacting motor coordination.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Developmental Biology

Background:

  • The angiomotin (Amot)-Yes-associated protein 1 (Yap1) complex regulates cell contact, polarity, and growth.
  • The specific roles of Amot and Yap1 in the central nervous system are not well understood.

Purpose of the Study:

  • To investigate the function of Amot and Yap1 in neuronal development, particularly dendritic morphogenesis.
  • To elucidate the molecular mechanisms underlying Amot and Yap1's role in dendrite growth.

Main Methods:

  • Utilized cultured hippocampal cells and Purkinje cells.
  • Performed conditional deletion of Amot and Yap1 in neurons.
  • Analyzed dendritic complexity, cerebellar morphology, and motor coordination.

Main Results:

  • Amot mediates dendritic morphogenesis in hippocampal and Purkinje cells.
  • Amot and Yap1 interaction is essential for dendrite growth and arborization.
  • Conditional deletion of Amot and Yap1 resulted in reduced dendritic complexity, abnormal cerebellar morphology, and motor deficits.
  • Amot/Yap1 function in dendrite development is independent of TEAD transcription factors and Hippo pathway genes.
  • Amot and Yap1 regulate dendrite development via phosphorylation of S6 kinase and S6 ribosomal protein.

Conclusions:

  • Amot and Yap1 are critical for proper dendritic development and cerebellar structure.
  • The Amot-Yap1 complex influences motor coordination through its role in neuronal development.
  • This pathway regulates dendrite growth independent of canonical Hippo pathway signaling, acting through S6 kinase phosphorylation.

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