期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 430, 期 18, 页码 3068-3080出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2018.07.002
关键词
Caspase-1; Caspase-11; Inflammasomes; Pyroptosis; Innate immunity
资金
- China Scholarship Council
- Australian National University
- Gretel and Gordon Bootes Medical Research Foundation
- National Health and Medical Research Council of Australia [APP1141504, APP1146864]
- R.G. Menzies Early Career Fellowship [APP1091544]
The Gasdermin (GSDM) family consists of Gasdermin A (GSDMA), Gasdermin B (GSDMB), Gasdermin C (GSDMC), Gasdermin D (GSDMD), Gasdermin E (GSDME) and Pejvakin (PJVK). GSDMD is activated by inflammasome-associated inflammatory caspases. Cleavage of GSDMD by human or mouse caspase-1, human caspase-4, human caspase-5, and mouse caspase-11 liberates the N-terminal effector domain from the C-terminal inhibitory domain. The N-terminal domain oligomerizes in the cell membrane and forms a pore of 10-16 nm in diameter, through which substrates of a smaller diameter, such as interleukin-1 beta and interleukin-1 beta, are secreted. The increasing abundance of membrane pores ultimately leads to membrane rupture and pyroptosis, releasing the entire cellular content. Other than GSDMD, the N-terminal domain of all GSDMs, with the exception of PJVK, have the ability to form pores. There is evidence to suggest that GSDMB and GSDME are cleaved by apoptotic caspases. Here, we review the mechanistic functions of GSDM proteins with respect to their expression and signaling profile in the cell, with more focused discussions on inflammasome activation and cell death. (C) 2018 Elsevier Ltd. All rights reserved.
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