GsdmD p30 elicited by caspase-11 during pyroptosis forms pores in membranes

Proceedings of the National Academy of Sciences of the United States of America

Volumn 113, Issue 28, 2016, Pages 7858-7863

  Aglietti, Robin A ^a   Estevez, Alberto ^a   Gupta, Aaron ^a   Ramirez, Monica Gonzalez ^b   Liu, Peter S ^a   Kayagaki, Nobuhiko ^a   Ciferri, Claudio ^a   Dixit, Vishva M ^a   Dueber, Erin C ^a  

^a GENENTECH INC   (United States)

^b BURNHAM INSTITUTE   (United States)

Author keywords

Caspase 11; GsdmD; Pyroptosis

Indexed keywords

CALCIUM; CASPASE 11; CYTOPLASM PROTEIN; GASDERMIN D P20; GASDERMIN D P30; LIPOPOLYSACCHARIDE; LIPOSOME; OLIGOMER; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; CASPASE; CASPASE 11, HUMAN; GSDMD PROTEIN, HUMAN; TUMOR PROTEIN;

ANIMAL CELL; AQUEOUS SOLUTION; ARTICLE; BONE MARROW DERIVED MACROPHAGE; CALCIUM TRANSPORT; CARBOXY TERMINAL SEQUENCE; CELL KILLING; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CHANNEL GATING; CONTROLLED STUDY; ELECTRON MICROSCOPY; ENZYME ACTIVATION; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; IN VITRO STUDY; LIPID BILAYER; MOUSE; MUTANT; NONHUMAN; OLIGOMERIZATION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PYROPTOSIS; TRANSIENT EXPRESSION; ANIMAL; HEK293 CELL LINE; METABOLISM; MUTATION; PHYSIOLOGY;

ANIMALS; CASPASES; HEK293 CELLS; HUMANS; LIPOSOMES; MICE; MUTATION; NEOPLASM PROTEINS; PYROPTOSIS;

EID: 84978128481     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1607769113     Document Type: Article

References (27)

1. Cookson BT, Brennan MA (2001) Pro-inflammatory programmed cell death. Trends Microbiol 9(3):113-114.
2. Lamkanfi M, Dixit VM (2014) Mechanisms and functions of inflammasomes. Cell 157(5):1013-1022.
3. Miao EA, et al. (2010) Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat Immunol 11(12):1136-1142.
4. Kayagaki N, et al. (2011) Non-canonical inflammasome activation targets caspase-11. Nature 479(7371):117-121.
5. Kayagaki N, et al. (2013) Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science 341(6151):1246-1249.
6. Hagar JA, Powell DA, Aachoui Y, Ernst RK, Miao EA (2013) Cytoplasmic LPS activates caspase-11: Implications in TLR4-independent endotoxic shock. Science 341(6151):1250-1253.
7. Shi J, et al. (2014) Inflammatory caspases are innate immune receptors for intracellular LPS. Nature 514(7521):187-192.
8. Shi J, et al. (2015) Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature 526(7575):660-665.
9. Kayagaki N, et al. (2015) Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature 526(7575):666-671.
10. Dal Peraro M, van der Goot FG (2016) Pore-forming toxins: Ancient, but never really out of fashion. Nat Rev Microbiol 14(2):77-92.
11. Tilley SJ, Orlova EV, Gilbert RJ, Andrew PW, Saibil HR (2005) Structural basis of pore formation by the bacterial toxin pneumolysin. Cell 121(2):247-256.
12. Leung C, et al. (2014) Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin. eLife 3:e04247.
13. Fink SL, Cookson BT (2006) Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages. Cell Microbiol 8(11):1812-1825.
14. Bergsbaken T, Fink SL, Cookson BT (2009) Pyroptosis: Host cell death and inflammation. Nat Rev Microbiol 7(2):99-109.
15. Lin HY, Lin PH, Wu SH, Yang LT (2015) Inducible expression of gasdermin A3 in the epidermis causes epidermal hyperplasia and skin inflammation. Exp Dermatol 24(11):897-899.
16. Yu J, et al. (2014) Inflammasome activation leads to Caspase-1-dependent mitochondrial damage and block of mitophagy. Proc Natl Acad Sci USA 111(43):15514-15519.
17. Giddings KS, Johnson AE, Tweten RK (2003) Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins. Proc Natl Acad Sci USA 100(20):11315-11320.
18. Shimada Y, Maruya M, Iwashita S, Ohno-Iwashita Y (2002) The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains. Eur J Biochem 269(24):6195-6203.
19. Waheed AA, et al. (2001) Selective binding of perfringolysin O derivative to cholesterol-rich membrane microdomains (rafts). Proc Natl Acad Sci USA 98(9):4926-4931.
20. Abrami L, van Der Goot FG (1999) Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin. J Cell Biol 147(1):175-184.
21. Brown DA, Rose JK (1992) Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68(3):533-544.
22. Zech T, et al. (2009) Accumulation of raft lipids in T-cell plasma membrane domains engaged in TCR signalling. EMBO J 28(5):466-476.
23. Renner LD, Weibel DB (2011) Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes. Proc Natl Acad Sci USA 108(15):6264-6269.
24. Sorice M, et al. (2009) Cardiolipin-enriched raft-like microdomains are essential activating platforms for apoptotic signals on mitochondria. FEBS Lett 583(15):2447-2450.
25. Oosawa F, Asakura S (1975) Thermodynamics of the Polymerization of Protein (Academic Press, New York).
26. Tamura M, et al. (2007) Members of a novel gene family, Gsdm, are expressed exclusively in the epithelium of the skin and gastrointestinal tract in a highly tissue-specific manner. Genomics 89(5):618-629.
27. Hildebrand JM, et al. (2014) Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death. Proc Natl Acad Sci USA 111(42):15072-15077.