Linking planar polarity signaling directly to actomyosin contractility during vertebrate neurulation

ABSTRACT: Actomyosin contractility represents an ancient feature of eukaryotic cells participating in many developmental and homeostasis events, including tissue morphogenesis, muscle contraction, and cell migration, with dysregulation implicated in various pathological conditions, such as cancer. At the molecular level, actomyosin comprises actin bundles and myosin motor proteins that are sensitive to posttranslational modifications like phosphorylation. While the molecular components of actomyosin and its regulation are well understood, the coordination of contractility by extracellular and intracellular signals, particularly from cellular signaling pathways, remains incompletely elucidated. This study focuses on planar cell polarity (PCP) signaling, previously associated with actomyosin contractility during vertebrate neurulation. Contrary to previous studies, our investigation reveals that main cytoplasmic PCP proteins, Prickle and Dishevelled, interact directly with key actomyosin components such as myosin light chain (MLC), leading to its phosphorylation and localized activation. Through relevant in vitro and in vivo models, we demonstrate that these PCP proteins function not merely passively and indirectly as previously reported, but that they actively control actomyosin contractility by acting as scaffold proteins, orchestrating the necessary machinery for contractility. These findings unveil a direct link of PCP signaling in crucial actomyosin contractility processes through MLC that are relevant to vertebrate neurulation and potentially beyond.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Canis Familiaris (dog) (canis Lupus Familiaris)

TISSUE(S): Mdck Cell

SUBMITTER: Pavel Roudnický  

LAB HEAD: Zbynek Zdrahal

PROVIDER: PXD052350 | Pride | 2024-09-19

REPOSITORIES: pride