Just So Stories about the Evolution of Apoptosis

Green, Douglas R.; Fitzgerald, Patrick

doi:10.1016/j.cub.2016.05.023

Cited by 58 publications

(48 citation statements)

References 64 publications

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“…83, 84 The critical argument against accepting the homology of caspases and metacaspases lies in the differences in protease activation. Specifically, metacaspase enzymes do not require dimerization or the presence of adaptor proteins, as is the case for metazoan caspases.…”

Section: The Evolutionary Origin and Utility Of Caspase-mediated Signmentioning

confidence: 99%

Evolution of caspase-mediated cell death and differentiation: twins separated at birth

2017

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The phenotypic and biochemical similarities between caspase-mediated apoptosis and cellular differentiation are striking. They include such diverse phenomenon as mitochondrial membrane perturbations, cytoskeletal rearrangements and DNA fragmentation. The parallels between the two disparate processes suggest some common ancestry and highlight the paradoxical nature of the death-centric view of caspases. That is, what is the driving selective pressure that sustains death-inducing proteins throughout eukaryotic evolution? Plausibly, caspase function may be rooted in a primordial non-death function, such as cell differentiation, and was co-opted for its role in programmed cell death. This review will delve into the links between caspase-mediated apoptosis and cell differentiation and examine the distinguishing features of these events. More critically, we chronicle the evolutionary origins of caspases and propose that caspases may have held an ancient role in mediating the fidelity of cell division/differentiation through its effects on proteostasis and protein quality control.

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Section: The Evolutionary Origin and Utility Of Caspase-mediated Signmentioning

confidence: 99%

Evolution of caspase-mediated cell death and differentiation: twins separated at birth

2017

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“…Moreover, phosphorylation of the serine residue on the C-terminus of human PDCD5 regulated its ability to induce apoptosis (Salvi et al, 2009). However, the process of apoptosis has still not been found in an organism other than an eukaryote (Green & Fitzgerald, 2016;Seth-Pasricha et al, 2013), and from the amino-acid sequence alignment there is no serine residue at the corresponding location in the archaeal PDCD5 homologs (Fig. 1a).…”

Section: Resultsmentioning

confidence: 99%

Crystal structure of the programmed cell death 5 protein from Sulfolobus solfataricus

et al. 2019

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Programmed cell death 5 (PDCD5) is a vital signaling protein in the apoptosis pathway in eukaryotes. It is known that there are two dissociated N‐terminal regions and a triple‐helix core in eukaryotic PDCD5. Structural and functional studies of PDCD5 from hyperthermophilic archaea have been limited to date. Here, the PDCD5 homolog Sso0352 (SsoPDCD5) was identified in Sulfolobus solfataricus, the SsoPDCD5 protein was expressed and crystallized, and the phase was identified by single‐wavelength anomalous diffraction. The native SsoPDCD5 crystal belonged to space group C2 and diffracted to 1.49 Å resolution. This is the first crystal structure of a PDCD5 homolog to be solved. SsoPDCD5 shares a similar triple‐helix bundle with eukaryotic PDCD5 but has a long α‐helix in the N‐terminus. A structural search and biochemical data suggest that SsoPDCD5 may function as a DNA‐binding protein.

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“…This could then have induced an evolutionary "battle" where the proteobacterium may have employed membrane pore forming molecules (such as Bcl--2 family members are) and injected toxins into the cytoplasm of the archaea, e.g. holocytochrome c. However, Bcl--2 like proteins are only found in animals and thus a large gap is evident between the evolution of the first eukaryotic cells and the evolution of multicellular animals that perform apoptotic cell death (recently reviewed by (Green and Fitzgerald, 2016). TMBIMP--family proteins could fulfil similar functions that are allocated to Bcl--2 family proteins in animals.…”

Section: Discussionmentioning

confidence: 99%