Format

Send to

Choose Destination
Nat Commun. 2019 Sep 2;10(1):3940. doi: 10.1038/s41467-019-11963-7.

Misshapen coordinates protrusion restriction and actomyosin contractility during collective cell migration.

Author information

1
Institute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montréal, QC, Canada.
2
Department of Pathology and Cell Biology, Faculty of Medicine, Université de Montréal, Montréal, QC, Canada.
3
Institute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montréal, QC, Canada. gregory.emery@umontreal.ca.
4
Department of Pathology and Cell Biology, Faculty of Medicine, Université de Montréal, Montréal, QC, Canada. gregory.emery@umontreal.ca.

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.

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center