Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition

Shin, Seung-Wook; Shimizu, Nobujiro; Tokoro, Mikiko; Nishikawa, Satoshi; Hatanaka, Y.; Anzai, Masayuki; Hamazaki, Jun; Kishigami, Satoshi; Saeki, Kazuhiro; Hosoi, Yoshihiko; Iritani, Akira; Murata, Shigeo; Matsumoto, Kazuya

doi:10.1242/bio.20123020

Cited by 31 publications

(38 citation statements)

References 53 publications

(92 reference statements)

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“…Irregular or incomplete activation of the embryonic genome will alter the processes required to direct normal embryo development. During MZT, the oocyte’s maternal mRNAs gradually undergo degradation along with gradual activation of the zygotic genes [ 45 ]. In this study, maternal degradation profiles differed between PBNT embryos with 2650 genes and BBNT embryos with 3822 genes;, 1515 genes were uniquely downregulated in BBNT embryos whereas there were 343 in PBNT embryos.…”

Section: Discussionmentioning

confidence: 99%

Irregular transcriptome reprogramming probably causes thec developmental failure of embryos produced by interspecies somatic cell nuclear transfer between the Przewalski’s gazelle and the bovine

Zuo

Gao

et al. 2014

BMC Genomics

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BackgroundInterspecies somatic cell nuclear transfer (iSCNT) has been regarded as a potential alternative for rescuing highly endangered species and can be used as a model for studying nuclear–cytoplasmic interactions. However, iSCNT embryos often fail to produce viable offspring. The alterations in normal molecular mechanisms contributing to extremely poor development are for the most part unknown.ResultsPrzewalski’s gazelle–bovine iSCNT embryos (PBNT) were produced by transferring Przewalski’s gazelle fibroblast nuclei into enucleated bovine oocytes. The percentages of PBNT embryos that developed to morula/blastocyst stages were extremely low even with the use of various treatments that included different SCNT protocols and treatment of embryos with small molecules. Transcriptional microarray analyses of the cloned embryos showed that the upregulation of reprogramming-associated genes in bovine–bovine SCNT (BBNT) embryos was significantly higher than those observed in PBNT embryos (1527:643). In all, 139 transcripts related to various transcription regulation factors (TFs) were unsuccessfully activated in the iSCNT embryos. Maternal degradation profiles showed that 1515 genes were uniquely downregulated in the BBNT embryos, while 343 genes were downregulated in the PBNT embryos. Incompatibilities between mitochondrial DNA (mtDNA) and nuclear DNA revealed that the TOMM (translocase of outer mitochondrial membrane)/TIMM (translocase of inner mitochondrial membrane) complex-associated genes in BBNT embryos had the highest expression levels, while the PBNT embryos exhibited much lower expression rates.ConclusionsImproper degradation of maternal transcripts, incomplete activation of TFs and abnormal expression of genes associated with mitochondrial function in PBNT embryos likely contributed to incomplete reprogramming of the donor cell nuclei and therefore led to the developmental failure of these cloned embryos.Electronic supplementary materialThe online version of this article (doi:10.1186/1471-2164-15-1113) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Irregular transcriptome reprogramming probably causes thec developmental failure of embryos produced by interspecies somatic cell nuclear transfer between the Przewalski’s gazelle and the bovine

Zuo

Gao

et al. 2014

BMC Genomics

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“…Additional trans -acting factors can also contribute. Proteins in the TRC/GET (transmembrane recognition complex in mammals/guided entry of tail-anchored proteins in yeast) pathway[65] and a zygote-specific proteasome assembly chaperone (ZPAC) in mouse[66] were shown to participate in eukaryotic CP assembly.…”

Section: The 20s Core Particle (Cp)mentioning

confidence: 99%

Proteasome Structure and Assembly

Budenholzer

Cheng

et al. 2017

Journal of Molecular Biology

315

280

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The eukaryotic 26S proteasome is a large multi-subunit complex that degrades the majority of proteins in the cell under normal conditions. The 26S proteasome can be divided into two subcomplexes: the 19S regulatory particle (RP) and the 20S core particle (CP). Most substrates are first covalently modified by ubiquitin, which then directs them to the proteasome. The function of the RP is to recognize, unfold, deubiquitylate and translocate substrates into the CP, which contains the proteolytic sites of the proteasome. Given the abundance and subunit complexity of the proteasome, the assembly of this ~2.5 MDa complex must be carefully orchestrated to ensure its correct formation. In recent years, significant advances have been made in the understanding of proteasome assembly, structure and function. Technical advances in cryo-electron microscopy have resulted in a series of atomic cryo-EM structures of both human and yeast 26S proteasomes. These structures have illuminated new intricacies and dynamics of the proteasome. In this review, we focus on the mechanisms of proteasome assembly, particularly in light of recent structural information.

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“…Whether all or part of the 33 proteasome subunits are induced is cell type‐dependent. All proteasome subunit genes are induced by activated Nrf1 after proteasome impairment (Radhakrishnan et al, ), whereas induction of a single subunit gene is sufficient for increasing proteasome activity in bone marrow stromal cells and embryonic stem cells (Lu et al, ; Shin et al, ; Vilchez, Boyer, et al, ). In the present study, functional proteasomes were remarkably induced by TCR stimulation, concomitant with the transcriptional up‐regulation of all proteasome subunits (Figure ).…”

Section: Discussionmentioning

confidence: 99%

Defective induction of the proteasome associated with T‐cell receptor signaling underlies T‐cell senescence

et al. 2019

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The proteasome degradation machinery is essential for a variety of cellular processes including senescence and T‐cell immunity. Decreased proteasome activity is associated with the aging process; however, the regulation of the proteasome in CD4+ T cells in relation to aging is unclear. Here, we show that defects in the induction of the proteasome in CD4+ T cells upon T‐cell receptor (TCR) stimulation underlie T‐cell senescence. Proteasome dysfunction promotes senescence‐associated phenotypes, including defective proliferation, cytokine production and increased levels of PD‐1+ CD44High CD4+ T cells. Proteasome induction by TCR signaling via MEK‐, IKK‐ and calcineurin‐dependent pathways is attenuated with age and decreased in PD‐1+ CD44High CD4+ T cells, the proportion of which increases with age. Our results indicate that defective induction of the proteasome is a hallmark of CD4+ T‐cell senescence.

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Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition

Cited by 31 publications

References 53 publications

Irregular transcriptome reprogramming probably causes thec developmental failure of embryos produced by interspecies somatic cell nuclear transfer between the Przewalski’s gazelle and the bovine

Irregular transcriptome reprogramming probably causes thec developmental failure of embryos produced by interspecies somatic cell nuclear transfer between the Przewalski’s gazelle and the bovine

Proteasome Structure and Assembly

Defective induction of the proteasome associated with T‐cell receptor signaling underlies T‐cell senescence

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