Bibliographic Details
| Title: |
Control of cytoskeletal dynamics during cellular responses to pore forming toxins |
| Authors: |
Francisco Sarmento Mesquita, Cláudia Brito, Didier Cabanes, Sandra Sousa |
| Source: |
Communicative & Integrative Biology, Vol 10, Iss 5-6 (2017) |
| Publisher Information: |
Taylor & Francis Group, 2017. |
| Publication Year: |
2017 |
| Collection: |
LCC:Biology (General) |
| Subject Terms: |
actomyosin, blebbing, endoplasmic reticulum chaperone, listeriolysin O, plasma membrane repair, pore-forming toxin, Biology (General), QH301-705.5 |
| More Details: |
Following damage by pore forming toxins (PFTs) host cells engage repair processes and display profound cytoskeletal remodeling and concomitant plasma membrane (PM) blebbing. We have recently demonstrated that host cells utilize similar mechanisms to control cytoskeletal dynamics in response to PFTs and during cell migration. This involves assembly of cortical actomyosin bundles, reorganisation of the endoplasmic reticulum (ER) network, and the interaction between the ER chaperone Gp96 and the molecular motor Non-muscle Myosin Heavy Chain IIA (NMHCIIA). Consequently, Gp96 regulates actomyosin activity, PM blebbing and cell migration, and protects PM integrity against PFTs. In addition, we observed that PFTs increase association of Gp96 and ER vacuoles with the cell surface or within PM blebs loosely attached to the cell body. Similarly, gut epithelial cells damaged by PFTs in vivo were shown to release microvilli structures or directly purge cytoplasmic content. Cytoplasmic purging involves profound cytoskeletal remodeling and ER vacuolation, suggesting that our observations recapitulate recovery processes in vivo. Here, we discuss our findings in light of the current understanding of PM repair mechanisms and in vivo recovery responses to PFTs. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
1942-0889
19420889 |
| Relation: |
https://doaj.org/toc/1942-0889 |
| DOI: |
10.1080/19420889.2017.1349582 |
| Access URL: |
https://doaj.org/article/f81ecd42f30f4d4c92980b111fb44066 |
| Accession Number: |
edsdoj.f81ecd42f30f4d4c92980b111fb44066 |
| Database: |
Directory of Open Access Journals |
