Understanding CARD Tricks in Apoptosomes

Wang, Li; Qiao, Qi; Wu, Hao

doi:10.1016/j.str.2017.03.013

Cited by 8 publications

(8 citation statements)

References 11 publications

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“…The final APAF1 -like protein is very similar in architecture to human APAF1 (Table 1; Robertson et al, 2006). The CARD domain of APAF1 is important due to its interaction with the CARD domain of CASP9 (Wang et al, 2017). As mentioned previously, formation of the apoptosome can be blocked by AVEN which uses the BH1 domain of BCL2L1 to bind it and APAF1 to prevent activation of CASP9 by the apoptosome; all of which we found orthologs for (Table 1; Chau et al, 2000;Elmore, 2007).…”

Section: Apoptotic Genes In the Sea Urchin (S Purpuratus)supporting

confidence: 61%

Hormonal Regulation of Programmed Cell Death in Sea Urchin Metamorphosis

Wynen

Heyland

2021

Front. Ecol. Evol.

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Programmed cell death (PCD) has been identified as a key process in the metamorphic transition of indirectly developing organisms such as frogs and insects. Many marine invertebrate species with indirect development and biphasic life cycles face the challenge of completing the metamorphic transition of the larval body into a juvenile when they settle into the benthic habitat. Some key characteristics stand out during this transition in comparison to frogs and insects: (1) the transition is often remarkably fast and (2) the larval body is largely abandoned and few structures transition into the juvenile stage. In sea urchins, a group with a drastic and fast metamorphosis, development and destruction of the larval body is regulated by endocrine signals. Here we provide a brief review of the basic regulatory mechanisms of PCD in animals. We then narrow our discussion to metamorphosis with a specific emphasis on sea urchins with indirect life histories and discuss the function of thyroid hormones and histamine in larval development, metamorphosis and settlement of the sea urchin Strongylocentrotus purpuratus. We were able to annotate the large majority of PCD related genes in the sea urchin S. purpuratus and ongoing studies on sea urchin metamorphosis will shed light on the regulatory architecture underlying this dramatic life history transition. While we find overwhelming evidence for hormonal regulation of PCD in animals, especially in the context of metamorphosis, the mechanisms in many marine invertebrate groups with indirect life histories requires more work. Hence, we propose that studies of PCD in animals requires functional studies in whole organisms rather than isolated cells. We predict that future work, targeting a broader array of organisms will not only help to reveal important new functions of PCD but provide a fundamentally new perspective on its use in a diversity of taxonomic, developmental, and ecological contexts.

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Section: Apoptotic Genes In the Sea Urchin (S Purpuratus)supporting

confidence: 61%

Hormonal Regulation of Programmed Cell Death in Sea Urchin Metamorphosis

Wynen

Heyland

2021

Front. Ecol. Evol.

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“…2j–k , Supplementary Fig. 5c, d ) 2 , 24 , 28 , 29 . The definition of the Type I–III interface follows the naming convention first used in describing the MyDDosome complex 2 , and subsequently widely adopted in describing DD filaments, such as MAVS-CARD.…”

Section: Resultsmentioning

confidence: 99%

Structural basis for distinct inflammasome complex assembly by human NLRP1 and CARD8

Gong

Robinson

et al. 2021

Nat Commun

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Nod-like receptor (NLR) proteins activate pyroptotic cell death and IL-1 driven inflammation by assembling and activating the inflammasome complex. Closely related sensor proteins NLRP1 and CARD8 undergo unique auto-proteolysis-dependent activation and are implicated in auto-inflammatory diseases; however, their mechanisms of activation are not understood. Here we report the structural basis of how the activating domains (FIINDUPA-CARD) of NLRP1 and CARD8 self-oligomerize to assemble distinct inflammasome complexes. Recombinant FIINDUPA-CARD of NLRP1 forms a two-layered filament, with an inner core of oligomerized CARD surrounded by an outer ring of FIINDUPA. Biochemically, self-assembled NLRP1-CARD filaments are sufficient to drive ASC speck formation in cultured human cells—a process that is greatly enhanced by NLRP1-FIINDUPA which forms oligomers in vitro. The cryo-EM structures of NLRP1-CARD and CARD8-CARD filaments, solved here at 3.7 Å, uncover unique structural features that enable NLRP1 and CARD8 to discriminate between ASC and pro-caspase-1. In summary, our findings provide structural insight into the mechanisms of activation for human NLRP1 and CARD8 and reveal how highly specific signaling can be achieved by heterotypic CARD interactions within the inflammasome complexes.

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“…6). In the Apaf-1/Casp-9 complex core, three Apaf-1 CARDs form one turn to recruit three Casp-9 CARDs; due to the special assembly mode within the apoptosome, the complex assembly is not infinite but limited at up to a 4:4 complex (34)(35)(36)(37). All of the subunits in one turn use the type III interface, and the type I and type II interactions are responsible for contacts between Apaf-1 and Casp-9.…”

Section: Discussionmentioning

confidence: 99%

Cryo-EM structures of ASC and NLRC4 CARD filaments reveal a unified mechanism of nucleation and activation of caspase-1

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

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Canonical inflammasomes are cytosolic supramolecular complexes that activate caspase-1 upon sensing extrinsic microbial invasions and intrinsic sterile stress signals. During inflammasome assembly, adaptor proteins ASC and NLRC4 recruit caspase-1 through homotypic caspase recruitment domain (CARD) interactions, leading to caspase-1 dimerization and activation. Activated caspase-1 processes proinflammatory cytokines and Gasdermin D to induce cytokine maturation and pyroptotic cell death. Here, we present cryo-electron microscopy (cryo-EM) structures of NLRC4 CARD and ASC CARD filaments mediated by conserved three types of asymmetric interactions (types I, II, and III). We find that the CARDs of these two adaptor proteins share a similar assembly pattern, which matches that of the caspase-1 CARD filament whose structure we defined previously. These data indicate a unified mechanism for downstream caspase-1 recruitment through CARD-CARD interactions by both adaptors. Using structure modeling, we further show that full-length NLRC4 assembles via two separate symmetries at its CARD and its nucleotide-binding domain (NBD), respectively. ASC | NLRC4 | inflammasome | caspase-1 | CARD

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Understanding CARD Tricks in Apoptosomes

Cited by 8 publications

References 11 publications

Hormonal Regulation of Programmed Cell Death in Sea Urchin Metamorphosis

Hormonal Regulation of Programmed Cell Death in Sea Urchin Metamorphosis

Structural basis for distinct inflammasome complex assembly by human NLRP1 and CARD8

Cryo-EM structures of ASC and NLRC4 CARD filaments reveal a unified mechanism of nucleation and activation of caspase-1

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