Amarante-Mendes GP , Adjemian S , Branco LM , Zanetti LC , Weinlich R , Bortoluci KR .

	Figure 1. Apoptosis pathways. The Intrinsic Pathway of apoptosis is activated when intracellular “stresses,” such as DNA or cytoskeleton damage or absence of growth/survival factors, are “perceived” by BH3-only members of the Bcl-2 family. These molecules become activated and migrate to the mitochondria where they facilitate or actively induce the release of apoptogenic factors, such as cytochrome c and SMAC/Diablo, to the cytosol. Cytochrome c associates with APAF-1 and pro-caspase-9 to form the apoptosome, resulting in the activation of caspase-9, which activates the effector caspases-3, -6, and -7, responsible for the biochemical and morphological modifications associated to apoptosis. SMAC/Diablo participates by preventing inhibition of caspases by IAPs. The extrinsic pathway of apoptosis initiates by the engagement of Death Receptor by their cognate Death Receptor Ligands causing the formation of the Death-inducing signaling complex (DISC). DISC is formed by the intracellular portion of the Death Receptors, the adaptor proteins TRADD and/or FADD and the pro-caspase-8 (or pro-caspase-10). Activated caspase-8 may directly activate the effector caspases or process the BH3-only protein Bid. Truncated Bid migrates to mitochondria and activates the extrinsic pathway of apoptosis.
	Figure 2. Necroptosis signaling. Death Receptor (DR)-induced necroptosis requires RIPK1 kinase activity to recruit RIPK3 that, in turn, recruits and activates MLKL via phosphorylation of its pseudokinase domain. Once phosphorylated, MLKL oligomerizes and migrates to the plasma membrane, where it interacts with phosphatidylinositol phosphates and induces membrane destabilization and rupture. Necroptosis signaling mediated by TRIF, IFNR, and DAI can directly activate RIPK3 and, in this case, RIPK1 acts as a negative regulator, mostly by recruiting to the signaling platform the suppressive complex containing Caspase-8, FADD and c-FLIP.
	Figure 3. Molecular basis of pyroptosis. (A) Canonical inflammasome assembly upon sensing of PAMPs, DAMPs or other cytosolic disturbs leads to the recruitment and activation of caspase-1 directly or via the recruitment of the adaptor protein ASC. Caspase-1 induces the maturation of pro-IL-1β and pro-IL-18 into their active forms as well as cleavage of Gasdermin D (GSDMD). The GSDMD pore form domain (PFD) interacts with the plasma membrane to form the GSDMD pore, leading to the release of the intracellular content, including IL-1β and IL-18. (B) Non-canonical inflammasome activation is initiated by the detection of cytosolic LPS from gram-negative bacteria by the pro-caspase-11 itself. Activated caspase-11 (caspase-4 or caspase-5 in humans), in turn, induces GSDMD cleavage and consequent pyroptosis.
	Figure 4. Interplay between PRRs and cell death mechanisms. The engagement of PRRs in response to PAMPs induces the activation of different cell death machineries in order to promote tissue homeostasis and host-defense against pathogens. Importantly, cell death products known collectively as DAMPs forms a feedback loop that stimulate PRRs to induce inflammatory/immune responses.

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