Identification of a novel gene family, paralogs of inhibitor of apoptosis proteins present in plants, fungi, and animals

Higashi, Katsumi; Takasawa, Ryoko; Yoshimori, Atsushi; Goh, Thary Gazi; Tanuma, Sei–ichi; Kuchitsu, Kazuyuki

doi:10.1007/s10495-005-1876-1

Cited by 19 publications

(46 citation statements)

References 56 publications

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“…The cell death mechanisms in plants are not as well defined as they are in mammals. This is due primarily to the lack of protein orthologs between mammals and plants for apoptosis signaling (39). It is likely that Grxs play a role in regulating apoptosis in plants; however, additional research on apoptotic mechanisms and the interaction between critical proteins and Grx in plants is compulsory before any definitive conclusions can be made.…”

Section: Plant Grxsmentioning

confidence: 99%

Protein-Thiol Oxidation and Cell Death: Regulatory Role of Glutaredoxins

Allen

Mieyal

2012

Antioxidants & Redox Signaling

146

135

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Apoptosis is a highly complex, tightly regulated process involving many different checks and balances. The influence of Grx activity on the interconnectivity among these various pathways remains unknown. Knowledge of the effects of Grx is essential for developing novel therapeutic approaches for treating diseases involving dysregulated apoptosis, such as cancer, heart disease, diabetes, and neurodegenerative diseases, where alterations in redox homeostasis are hallmarks for pathogenesis.

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Section: Plant Grxsmentioning

confidence: 99%

Protein-Thiol Oxidation and Cell Death: Regulatory Role of Glutaredoxins

Allen

Mieyal

2012

Antioxidants & Redox Signaling

146

135

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“…IAPs are metalloproteins that contain one or more zinc-binding motifs referred to as baculovirus IAP repeats and a RING (really interesting new gene) domain (105). First described in baculoviruses (24,27), cellular homologues of IAPs have been reported in organisms ranging from yeasts to humans and, most recently, plants (51). Many IAPs are known to function by directly inhibiting caspases, thereby halting the execution phase of programmed cell death (105) and maximizing efficiency of viral replication (24).…”

Section: Vol 80 2006mentioning

confidence: 99%

Genomic Sequence of Spodoptera frugiperda Ascovirus 1a , an Enveloped, Double-Stranded DNA Insect Virus That Manipulates Apoptosis for Viral Reproduction

Bideshi

Demattei

Rouleux‐Bonnin

et al. 2006

J Virol

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Ascoviruses (family Ascoviridae) are double-stranded DNA viruses with circular genomes that attack lepidopterans, where they produce large, enveloped virions, 150 by 400 nm, and cause a chronic, fatal disease with a cytopathology resembling that of apoptosis. After infection, host cell DNA is degraded, the nucleus fragments, and the cell then cleaves into large virion-containing vesicles. These vesicles and virions circulate in the hemolymph, where they are acquired by parasitic wasps during oviposition and subsequently transmitted to new hosts. To develop a better understanding of ascovirus biology, we sequenced the genome of the type species Spodoptera frugiperda ascovirus 1a (SfAV-1a). The genome consisted of 156,922 bp, with a G؉C ratio of 49.2%, and contained 123 putative open reading frames coding for a variety of enzymes and virion structural proteins, of which tentative functions were assigned to 44. Among the most interesting enzymes, due to their potential role in apoptosis and viral vesicle formation, were a caspase, a cathepsin B, several kinases, E3 ubiquitin ligases, and especially several enzymes involved in lipid metabolism, including a fatty acid elongase, a sphingomyelinase, a phosphate acyltransferase, and a patatin-like phospholipase. Comparison of SfAV-1a proteins with those of other viruses showed that 10% were orthologs of Chilo iridescent virus proteins, the highest correspondence with any virus, providing further evidence that ascoviruses evolved from a lepidopteran iridovirus. The SfAV-1a genome sequence will facilitate the determination of how ascoviruses manipulate apoptosis to generate the novel virion-containing vesicles characteristic of these viruses and enable study of their origin and evolution.The family Ascoviridae was erected recently to accommodate several new species of large double-stranded DNA (dsDNA) viruses with circular genomes that attack insects of the order Lepidoptera at the larval and pupal stages, causing a chronic, fatal disease (38). Viruses of this family are characterized by large, enveloped virions with a distinctive reticulate surface pattern. Depending on the species, virions are either bacilliform or allantoid (sausage shaped), contain an internal lipid membrane surrounding the DNA/protein core, and are composed of at least 12 structural proteins, ranging in mass from 10 to 200 kDa (40).These structural characteristics of the virions are sufficient to distinguish ascoviruses from all other large dsDNA viruses. However, the most novel feature of ascoviruses is not their virion structure, but rather their unusual cellular pathology and transmission. Unlike for all other viruses, a variety of evidence suggests that ascoviruses induce apoptosis as part of a mechanism that enhances their reproduction and transmission. A typical pattern of cytopathology, as exemplified by Spodoptera frugiperda ascovirus 1a (SfAV-1a), the type species, begins with nuclear hypertrophy and cleavage of host DNA, followed by lysis of the nucleus and fragmentation of the nuclear memb...

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“…Homologues of baculoviral IAP have been found in a number of eukaryotic organisms, such as yeast, drosophila, human and, most recently, plants (8). In mammals, there are eight types of IAPs (Fig.…”

Section: Ring-containing Iaps Couple Apoptosis and Ubiquitylationmentioning

confidence: 99%

“…The IAP proteins were originally identified in baculovirus, because of their ability to suppress apoptosis in infected host cells (7). Homologues of baculoviral IAP have been found in a number of eukaryotic organisms, such as yeast, drosophila, human and, most recently, plants (8). In mammals, there are eight types of IAPs ( Fig.…”

Section: Ring-containing Iaps Couple Apoptosis and Ubiquitylationmentioning

confidence: 99%

The ubiquitin ligase ability of IAPs regulates apoptosis

Zou

2005

IUBMB Life (International Union of Biochemistry and Molecular B

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SummaryAccumulating evidence indicates that there is a critical role of the ubiquitin/proteasome pathway in the regulation of apoptosis. Among the important molecules that couple these two fundamental cellular activities are members of the inhibitor of apoptosis (IAP) protein family. In addition to their well-studied ability to directly bind and inhibit caspases, many IAPs contain RING domains that are necessary and sufficient to cause ubiquitylation and subsequent proteasome-mediated proteolysis. This review summarizes recent findings about the ubiquitin protein ligase activity of IAPs, and considers possible mechanisms for substrate selectivity.IUBMB Life, 57: 779 -786, 2005

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Identification of a novel gene family, paralogs of inhibitor of apoptosis proteins present in plants, fungi, and animals

Cited by 19 publications

References 56 publications

Protein-Thiol Oxidation and Cell Death: Regulatory Role of Glutaredoxins

Protein-Thiol Oxidation and Cell Death: Regulatory Role of Glutaredoxins

Genomic Sequence of Spodoptera frugiperda Ascovirus 1a , an Enveloped, Double-Stranded DNA Insect Virus That Manipulates Apoptosis for Viral Reproduction

The ubiquitin ligase ability of IAPs regulates apoptosis

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