The balbiani body and the concept of physiological amyloids

Böke, Elvan; Mitchison, Timothy J.

doi:10.1080/15384101.2016.1241605

Cited by 29 publications

(22 citation statements)

References 7 publications

(13 reference statements)

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“…For example, the PrLD of RBM14 (as well as FUS) is critical for paraspeckle formation [154]. Likewise, the PrLD of hnRNPD plays an important role in Sam68 nuclear body formation [155], whereas the PrLD of Xvelo is critical for Balbiani body formation [156,157]. Finally, PrLDs in DAZ1-4 and DAZL are predicted to have important roles in the formation of amyloid-like structures that regulate key meiotic events [158,159].…”

Section: Disease-associated Rbps Are Involved In the Formation Of Rnpmentioning

confidence: 99%

RNA-binding proteins with prion-like domains in health and disease

Harrison

Shorter

2017

Biochemical Journal

368

424

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Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD). PrLDs are low-complexity domains that possess a similar amino acid composition to prion domains in yeast, which enable several proteins, including Sup35 and Rnq1, to form infectious conformers, termed prions. In humans, PrLDs contribute to RBP function and enable RBPs to undergo liquid–liquid phase transitions that underlie the biogenesis of various membraneless organelles. However, this activity appears to render RBPs prone to misfolding and aggregation connected to neurodegenerative disease. Indeed, numerous RBPs with PrLDs, including TDP-43 (transactivation response element DNA-binding protein 43), FUS (fused in sarcoma), TAF15 (TATA-binding protein-associated factor 15), EWSR1 (Ewing sarcoma breakpoint region 1), and heterogeneous nuclear ribo-nucleoproteins A1 and A2 (hnRNPA1 and hnRNPA2), have now been connected via pathology and genetics to the etiology of several neurodegenerative diseases, including amyotrophic lateral sclerosis, frontotemporal dementia, and multisystem proteinopathy. Here, we review the physiological and pathological roles of the most prominent RBPs with PrLDs. We also highlight the potential of protein disaggregases, including Hsp104, as a therapeutic strategy to combat the aberrant phase transitions of RBPs with PrLDs that likely underpin neurodegeneration.

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Section: Disease-associated Rbps Are Involved In the Formation Of Rnpmentioning

confidence: 99%

RNA-binding proteins with prion-like domains in health and disease

Harrison

Shorter

2017

Biochemical Journal

368

424

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“…Another type of RNA storage compartment identified in oocytes are Balbiani bodies: Large membrane-less cytoplasmic organelles that were initially described in dormant Xenopus oocytes in which they were found to contain Golgi elements, mitochondria, and endoplasmic reticulum as well as RNA [29]. Such structures have been reported to exist in oocytes of other vertebrate species, although in mice they have been identified only in very young oocytes, and these have not been found to contain RNA [30].…”

Section: Oocyte Rbps and Post-transcriptional Regulationmentioning

confidence: 99%

Diversity of RNA-Binding Proteins Modulating Post-Transcriptional Regulation of Protein Expression in the Maturing Mammalian Oocyte

Christou‐Kent

Dhellemmes

Lambert

et al. 2020

Cells

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The oocyte faces a particular challenge in terms of gene regulation. When oocytes resume meiosis at the end of the growth phase and prior to ovulation, the condensed chromatin state prevents the transcription of genes as they are required. Transcription is effectively silenced from the late germinal vesicle (GV) stage until embryonic genome activation (EGA) following fertilisation. Therefore, during its growth, the oocyte must produce the mRNA transcripts needed to fulfil its protein requirements during the active period of meiotic completion, fertilisation, and the maternal-to zygote-transition (MZT). After meiotic resumption, gene expression control can be said to be transferred from the nucleus to the cytoplasm, from transcriptional regulation to translational regulation. Maternal RNA-binding proteins (RBPs) are the mediators of translational regulation and their role in oocyte maturation and early embryo development is vital. Understanding these mechanisms will provide invaluable insight into the oocyte's requirements for developmental competence, with important implications for the diagnosis and treatment of certain types of infertility. Here, we give an overview of post-transcriptional regulation in the oocyte, emphasising the current knowledge of mammalian RBP mechanisms, and develop the roles of these mechanisms in the timely activation and elimination of maternal transcripts.

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“…Enter BB. First recognized to be comprised of amyloid-like proteins, whose storage and function would play out during the development of frog oocytes [3] there is now good reason to believe that a similar modus operandi may be shared by the oocytes of mammals including humans. At least this is what the paper by Pimentel and coworkers would like us to believe (Amyloid-like substance in mice and human oocytes and embryos https://doi.org/10.…”

mentioning

confidence: 99%

Phase transitions in human ARTs: fertility preservation comes of age

Albertini

2019

J Assist Reprod Genet

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The balbiani body and the concept of physiological amyloids

Cited by 29 publications

References 7 publications

RNA-binding proteins with prion-like domains in health and disease

RNA-binding proteins with prion-like domains in health and disease

Diversity of RNA-Binding Proteins Modulating Post-Transcriptional Regulation of Protein Expression in the Maturing Mammalian Oocyte

Phase transitions in human ARTs: fertility preservation comes of age

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