期刊
AUTOPHAGY
卷 12, 期 12, 页码 2508-2509出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2016.1235126
关键词
antibacterial autophagy; NDP52; optineurin; PI(3)P; Salmonella; TBK1; WIPI
类别
资金
- MRC [MC_U105170648] Funding Source: UKRI
- Wellcome Trust [104752/Z/14/Z] Funding Source: researchfish
- Medical Research Council [MC_U105170648] Funding Source: Medline
Defense of the mammalian cell cytosol against Salmonella invasion is reliant upon capture of the infiltrating bacteria by macroautophagy (hereafter autophagy), a process controlled by the kinase TBK1. In our recent study we showed that recruitment of TBK1 activity to Salmonella stabilizes the key autophagy regulator WIPI2 on those bacteria, a novel and essential function for TBK1 in the control of the early steps of antibacterial autophagy. Substantial redundancy exists in the precise recruitment mechanism for TBK1 because engagement with any of several Salmonella-associated eat-me' signals, including host-derived glycans, and K48- and K63-linked ubiquitin chains, suffices to recruit TBK1 functionality. We therefore propose that buffering TBK1 recruitment against potential bacterial interference might be of evolutionary advantage to the host.
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