Caspase-8: Arbitrating Life and Death in the Innate Immune System

被引:0
作者
Gupta, Sahil [1 ,2 ,3 ]
Lopez, Monica Aida [2 ]
Ektesabi, Amin M. [2 ,3 ]
Tsoporis, James N. [2 ]
Vaswani, Chirag M. [2 ,4 ]
Gandhi, Shil Y. [1 ]
Fairn, Gregory D. [2 ,5 ]
Dos Santos, Claudia C. [2 ,3 ,4 ]
Marshall, John C. [2 ,3 ,6 ]
机构
[1] Univ Queensland, Fac Med, Med Sch, Brisbane, Qld 4006, Australia
[2] St Michaels Hosp, Unity Hlth Toronto, Keenan Res Ctr Biomed Sci, Toronto, ON M5B 1W8, Canada
[3] Univ Toronto, Inst Med Sci, Temerty Fac Med, Toronto, ON M5S 3K3, Canada
[4] Univ Toronto, Temerty Fac Med, Dept Physiol, Toronto, ON M5S 3K3, Canada
[5] Dalhousie Univ, Dept Pathol, Halifax, NS B3H 4R2, Canada
[6] St Michaels Hosp, Unity Hlth Toronto, Dept Crit Care Med, Toronto, ON M5B 1W8, Canada
关键词
caspase-8; apoptosis; inflammation; alternative splicing; post-translational modification; PROGRAMMED CELL-DEATH; NEUTROPHIL SURVIVAL; SRC KINASE; APOPTOSIS; PHOSPHORYLATION; ACTIVATION; EFFECTOR; POLYUBIQUITINATION; DEPHOSPHORYLATION; UBIQUITINATION;
D O I
10.3390/cells14040240
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The canonical function of caspase-8 is to control timely cellular apoptosis to maintain tissue homeostasis and clear dysfunctional cells; however, emerging findings reveal novel, non-canonical roles of caspase in addition to regulating cellular apoptosis, including inflammatory response regulation, immune function, and cell differentiation. Furthermore, the functional versatility of caspase-8 is reported to be contingent on the presence and dimerization of various isoforms, which are produced through alternative splicing, altering its function and protein-protein interactions. Equally important are post-translational modifications, including phosphorylation and ubiquitination, which can act as a nexus to control caspase-8 activity and cellular localization. Here, we review the alternative splicing and post-translational modifications made to caspase-8 and discuss their influence on its canonical and non-canonical roles.
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页数:13
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共 65 条
  • [1] Galluzzi L., Vitale I., Aaronson S.A., Abrams J.M., Adam D., Agostinis P., Alnemri E.S., Altucci L., Amelio I., Andrews D.W., Et al., Molecular mechanisms of cell death: Recommendations of the Nomenclature Committee on Cell Death 2018, Cell Death Differ, 25, pp. 486-541, (2018)
  • [2] Shi J., Gao W., Shao F., Pyroptosis: Gasdermin-Mediated Programmed Necrotic Cell Death, Trends Biochem. Sci, 42, pp. 245-254, (2017)
  • [3] Orozco S., Yatim N., Werner M.R., Tran H., Gunja S.Y., Tait S.W.G., Albert M.L., Green D.R., Oberst A., RIPK1 both positively and negatively regulates RIPK3 oligomerization and necroptosis, Cell Death Differ, 21, pp. 1511-1521, (2014)
  • [4] Song H.J., Parodo J., Kapus A., Rotstein O.D., Marshall J.C., Dynamic regulation of neutrophil survival through tyrosine phosphorylation or dephosphorylation of caspase-8, J. Biol. Chem, 283, pp. 5402-5413, (2008)
  • [5] Jia S.H., Parodo J., Charbonney E., Tsang J.L.Y., Jia S.Y., Rotstein O.D., Kapus A., Marshall J.C., Activated neutrophils induce epithelial cell apoptosis through oxidant-dependent tyrosine dephosphorylation of caspase-8, Am. J. Pathol, 184, pp. 1030-1040, (2014)
  • [6] Gupta S., Lee C.M., Wang J.F., Parodo J., Jia S.H., Hu J., Marshall J.C., Heat-shock protein-90 prolongs septic neutrophil survival by protecting c-Src kinase and caspase-8 from proteasomal degradation, J. Leukoc. Biol, 103, pp. 933-944, (2018)
  • [7] Cursi S., Rufini A., Stagni V., Condo I., Matafora V., Bachi A., Bonifazi A.P., Coppola L., Superti-Furga G., Testi R., Et al., Src kinase phosphorylates Caspase-8 on Tyr380: A novel mechanism of apoptosis suppression, EMBO J, 25, (2006)
  • [8] Gupta S., Activation and Stabilization of the Caspase-8 Survivalsome Is Indispensable for Functional Toll-like Receptor 4 Dependent Signaling in Septic Neutrophils, Ph.D Thesis, (2020)
  • [9] Ellis H.M., Horvitz H.R., Genetic control of programmed cell death in the nematode C. elegans, Cell, 44, pp. 817-829, (1986)
  • [10] Chinnaiyan A.M., O'Rourke K., Lane B.R., Dixit V.M., Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death, Science, 275, pp. 1122-1126, (1997)