Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2015 Sep 28;1:15035. doi: 10.1038/cddiscovery.2015.35

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2015 Cell Death Differentiation Association

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

PMC Copyright notice

Proposed model of VacA effects on Cx43 and autophagy, followed by apoptosis. After VacA was translocated into cells via a lipid raft-dependent pathway, toxin channel activity is proposed to cause dysregulated GSH metabolism and activation of Rac1, followed by ERK phosphorylation (①–④). These signaling events promote Cx43 endocytosis. Cx43 enters endosome and pre-autophagy pathways as determined by the presence of several vesicle marker proteins (e.g., LC3, Atg16L1, EEA1 and LAMP1) (⑤–⑧). Cx43 accumulated in cytoplasmic compartments and colocalized with autophagosomal marker LC3 and VacA. The cytoplasmic compartments were predominantly localized in the Tx-insoluble fraction, suggesting its localization in cholesterol-rich DRMs (⑨–⑩). In contrast, LRP1-dependent endocytosis of VacA caused ROS-dependent autophagy and apoptosis (I–IV). These compartments were localized to the Tx-soluble fraction.