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. Author manuscript; available in PMC: 2020 Jun 18.
Published in final edited form as: Immunity. 2019 Jun 18;50(6):1352–1364. doi: 10.1016/j.immuni.2019.05.020

Figure 1. Functional classification and domain architecture of murine and human caspases.

Figure 1

The members of the caspase-family are classified as inflammatory or apoptotic based on the described functions and domain architecture. The caspases-1, 4, -5 and -11 are grouped as inflammatory caspases and share a CARD-domain at the N-terminal end. The apoptotic caspases can be further sub-categorized in initiator- and executioner caspases. The caspases-8, -9 and -10 have domain architecture akin to the inflammatory caspases, however, their function is to initiate apoptosis through the activation of the executioner caspases-3, -6 and -7. In addition, caspase-2 shares domain structures with the inflammatory caspases, however, its function is described to be cell cycle related. Structurally, murine caspase-12 clusters with the inflammatory caspases, however, until today its function remains undefined. Alternatively, for human caspase-12, it is generally accepted that 75% of the population is knock-out, while the remaining 25% carry a proteolytically inactive pseudoprotease (h*). The function of caspase-14 is linked to cell differentiation. m, murine and h, human.