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

Paolo Armando Gagliardi, Desiana Somale, Alberto Puliafito, Giulia Chiaverina, Laura di Blasio, Michele Oneto, Paolo Bianchini, Federico Bussolino, Luca Primo

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)231-249
Number of pages19
JournalJournal of Cell Biology
Volume217
Issue number1
DOIs
Publication statusPublished - Jan 1 2018

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Myotonic Dystrophy
Caspases
Actins
Phosphotransferases
Epithelial Cells
Actomyosin
Myosins
Cytoskeleton
Polymerization
Epithelium
Apoptosis

ASJC Scopus subject areas

  • Cell Biology

Cite this

MRCKα is activated by caspase cleavage to assemble an apical actin ring for epithelial cell extrusion. / Gagliardi, Paolo Armando; Somale, Desiana; Puliafito, Alberto; Chiaverina, Giulia; di Blasio, Laura; Oneto, Michele; Bianchini, Paolo; Bussolino, Federico; Primo, Luca.

In: Journal of Cell Biology, Vol. 217, No. 1, 01.01.2018, p. 231-249.

Research output: Contribution to journalArticle

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AU - Gagliardi, Paolo Armando

AU - Somale, Desiana

AU - Puliafito, Alberto

AU - Chiaverina, Giulia

AU - di Blasio, Laura

AU - Oneto, Michele

AU - Bianchini, Paolo

AU - Bussolino, Federico

AU - Primo, Luca

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AB - 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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