Korean J Physiol Pharmacol.  2025 Mar;29(2):129-138. 10.4196/kjpp.24.240.

Functional interplay between non-canonical inflammasomes and autophagy in inflammatory responses and diseases

• Yi YS

• KMID: 2565426
• DOI: http://doi.org/10.4196/kjpp.24.240

Abstract

The inflammasome is a cytosolic multiprotein platform that plays a key role in the inflammatory response, an essential innate immune response that protects the body from pathogens and cellular danger signals. Autophagy is a fundamental cellular mechanism that maintains homeostasis through the elimination and recycling of dysfunctional molecules and subcellular elements. Many previous studies have demonstrated a functional interplay between canonical inflammasomes that were earlier discovered and autophagy in inflammatory responses and diseases. Given the increasing evidence that non-canonical inflammasomes are unique and key factors in inflammatory responses, the functional interplay between non-canonical inflammasomes and autophagy is noteworthy. Recent studies have demonstrated that non-canonical inflammasomes and autophagy are functionally correlated with inflammatory responses and diseases. This review comprehensively discusses recent studies that have investigated the functional interplay of non-canonical inflammasomes, such as mouse caspase-11 and human caspase-4, with autophagy and autophagy-related proteins in inflammatory responses and diseases and provides insight into the development of novel anti-inflammatory therapeutics by modulating the functional interplay between non-canonical inflammasomes and autophagy.

Keyword

Autophagy; Caspase-4; Caspase-11; Inflammation; Non-canonical inflammasome

Figure

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  Fig. 1 Non-canonical inflammasomes and non-canonical inflammasome-activated inflammatory signaling pathways. (A) Domain structure of mouse caspase-11 and human caspase-4 and caspase-5. Caspase-11, caspase-4, and caspase-5 have same domain structure composed of amino-terminal CARDs, followed by large (p20) and small (p10) catalytic domains, but different amino acid lengths; 373, 377, and 434 amino acids, respectively. (B) Sensing of LPS by caspase-4/5/11. Caspase-4/5/11 senses cytosolic LPS by direct interaction between CARDs of caspase-4/5/11 and lipid A of LPS, which leads to the formation of LPS-caspase-4/5/11 complexes. (C) Non-canonical inflammasome-activated inflammatory signaling pathways. LPS derived from gram-negative bacteria is internalized into the host cells, and caspase-4/5/11 directly senses the cytosolic LPS, leading to the formation of LPS-caspase-4/5/11 complexes and caspase-4/5/11 non-canonical inflammasomes by oligomerization through CARD-CARD interaction. Caspase-4/5/11 non-canonical inflammasomes activated by autoproteolytic cleavage induce the proteolytic cleavage of GSDMD and the generation of GSDMD pores, resulting in pyroptosis of the cells. Caspase-4/5/11 non-canonical inflammasome activation induces NLRP3 inflammasome-mediated proteolytic activation of caspase-1, leading to the proteolytic maturation and secretion of IL-1β and IL-18 through GSDMD pores. CARD, caspase recruitment domain; LPS, lipopolysaccharide; GSDMD, gasdermin D; IL, interleukin.

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  Fig. 2 Summary of functional interplay between mouse caspase-11 non-canonical inflammasome and autophagy. (A) Inhibitory role of autophagy in caspase-11 non-canonical inflammasome during infection with vacuolar gram-negative bacteria in mouse macrophages. (B) Inhibitory role of autophagy in NRF2-mediated caspase-11 non-canonical inflammasome activation and HMGB1 release during inflammatory responses in hepatocytes. (C) Inhibitory role of autophagy-related proteins in caspase-11 non-canonical inflammasome in macrophages and LPS-induced acute lethal septic mice. (D) Induction of autophagy by caspase-11 non-canonical inflammasome in response to bacterial infection in the macrophages. HMGB1, high‐mobility group box 1; LPS, lipopolysaccharide; GBP, guanylate‐binding protein.

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  Fig. 3 Summary of functional interplay between human caspase-4 non-canonical inflammasome and autophagy. CMECs, cardiac microvascular endothelial cells.

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