Alternative human eIF5A protein isoform plays a critical role in mitochondria

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dc.contributor.authorPereira, Karina D. [UNESP]
dc.contributor.authorTamborlin, Letícia [UNESP]
dc.contributor.authorde Lima, Tanes I.
dc.contributor.authorConsonni, Silvio R.
dc.contributor.authorSilveira, Leonardo R.
dc.contributor.authorLuchessi, Augusto D. [UNESP]
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2021-06-25T10:20:29Z
dc.date.available2021-06-25T10:20:29Z
dc.date.issued2021-05-01
dc.description.abstractThe eukaryotic translation initiation factor 5A (eIF5A) is the only known protein containing the amino acid residue hypusine, essential for its activity. Hypusine residue is produced by a posttranslational modification involving deoxyhypusine synthetase and deoxyhypusine hydroxylase. Herein, we aimed to describe the role of the alternative human isoform A on mitochondrial processes. Isoform A depletion modulates oxidative metabolism in association with the downregulation of mitochondrial biogenesis-related genes. Through positive feedback, it increases cell respiration leading to highly reactive oxygen species production, which impacts mitochondrial bioenergetics. These metabolic changes compromise mitochondrial morphology, increasing its electron density and fission, observed by transmission electron microscopy. This set of changes leads the cells to apoptosis, evidenced by increased DNA fragmentation and proapoptotic BAK protein content increase. Thus, we show that the alternative eIF5A isoform A is crucial for energy metabolism controlled by mitochondria and cellular survival.en
dc.description.affiliationLaboratory of Biotechnology School of Applied Sciences University of Campinas (UNICAMP)
dc.description.affiliationInstitute of Biosciences São Paulo State University (UNESP)
dc.description.affiliationDepartment of Structural and Functional Biology Obesity and Comorbidities Research Center University of Campinas (UNICAMP)
dc.description.affiliationLaboratory of Cytochemistry and Immunocytochemistry Department of Biochemistry and Tissue Biology Institute of Biology University of Campinas (UNICAMP)
dc.description.affiliationUnespInstitute of Biosciences São Paulo State University (UNESP)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdFAPESP: 2010/18095-0
dc.description.sponsorshipIdFAPESP: 2013/23620-4
dc.description.sponsorshipIdFAPESP: 2017/21914-1
dc.description.sponsorshipIdFAPESP: 2019/06951-3
dc.format.extent549-561
dc.identifierhttp://dx.doi.org/10.1002/jcb.29884
dc.identifier.citationJournal of Cellular Biochemistry, v. 122, n. 5, p. 549-561, 2021.
dc.identifier.doi10.1002/jcb.29884
dc.identifier.issn1097-4644
dc.identifier.issn0730-2312
dc.identifier.scopus2-s2.0-85099410508
dc.identifier.urihttp://hdl.handle.net/11449/205744
dc.language.isoeng
dc.relation.ispartofJournal of Cellular Biochemistry
dc.sourceScopus
dc.subjectapoptosis
dc.subjecteIF5A isoform A
dc.subjecthuman
dc.subjecthypusine
dc.subjectmitochondria
dc.subjectoxidative metabolism
dc.titleAlternative human eIF5A protein isoform plays a critical role in mitochondriaen
dc.typeArtigo
unesp.author.orcid0000-0003-2080-3524[6]

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