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Merck
  • MRCKα is activated by caspase cleavage to assemble an apical actin ring for epithelial cell extrusion.

MRCKα is activated by caspase cleavage to assemble an apical actin ring for epithelial cell extrusion.

The Journal of cell biology (2017-11-23)
Paolo Armando Gagliardi, Desiana Somale, Alberto Puliafito, Giulia Chiaverina, Laura di Blasio, Michele Oneto, Paolo Bianchini, Federico Bussolino, Luca Primo
摘要

Extrusion of apoptotic cells from epithelial tissues requires orchestrated morphological rearrangements of the apoptotic cell and its neighbors. However, the connections between the apoptotic cascade and events leading to extrusion are not fully understood. Here, we characterize an apoptotic extrusion apical actin ring (EAAR) that is assembled within the apoptotic cell and drives epithelial extrusion. Caspase-mediated cleavage of myotonic dystrophy kinase-related CDC42-binding kinase-α (MRCKα) triggers a signaling pathway that leads to the assembly of EAAR that pulls actin bundles, resulting in the compaction and removal of the cell body. We provide a detailed portrait of the EAAR including F-actin flow, the contribution of myosin contraction, and actin polymerization at bundles' terminals when the product of MRCKα cleavage is expressed. These results add to our understanding of the mechanisms controlling the process of epithelial extrusion by establishing a causal relationship between the triggering events of apoptosis, the activation of MRCKα, and its subsequent effects on the dynamics of actomyosin cytoskeleton rearrangement.

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Triton X-100, laboratory grade
Sigma-Aldrich
红海海绵素A, from sea sponge, ≥85% (HPLC), waxy solid
Sigma-Aldrich
BI-6C9, ≥97% (HPLC), solid