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Misshapen coordinates protrusion restriction and actomyosin contractility during collective cell migration

Author

Listed:
  • Cédric Plutoni

    (Université de Montréal)

  • Sarah Keil

    (Université de Montréal)

  • Carlos Zeledon

    (Université de Montréal)

  • Lara Elis Alberici Delsin

    (Université de Montréal)

  • Barbara Decelle

    (Université de Montréal)

  • Philippe P. Roux

    (Université de Montréal
    Université de Montréal)

  • Sébastien Carréno

    (Université de Montréal
    Université de Montréal)

  • Gregory Emery

    (Université de Montréal
    Université de Montréal)

Abstract

Collective cell migration is involved in development, wound healing and metastasis. In the Drosophila ovary, border cells (BC) form a small cluster that migrates collectively through the egg chamber. To achieve directed motility, the BC cluster coordinates the formation of protrusions in its leader cell and contractility at the rear. Restricting protrusions to leader cells requires the actin and plasma membrane linker Moesin. Herein, we show that the Ste20-like kinase Misshapen phosphorylates Moesin in vitro and in BC. Depletion of Misshapen disrupts protrusion restriction, thereby allowing other cells within the cluster to protrude. In addition, we show that Misshapen is critical to generate contractile forces both at the rear of the cluster and at the base of protrusions. Together, our results indicate that Misshapen is a key regulator of BC migration as it coordinates two independent pathways that restrict protrusion formation to the leader cells and induces contractile forces.

Suggested Citation

  • Cédric Plutoni & Sarah Keil & Carlos Zeledon & Lara Elis Alberici Delsin & Barbara Decelle & Philippe P. Roux & Sébastien Carréno & Gregory Emery, 2019. "Misshapen coordinates protrusion restriction and actomyosin contractility during collective cell migration," Nature Communications, Nature, vol. 10(1), pages 1-16, December.
  • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11963-7
    DOI: 10.1038/s41467-019-11963-7
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