The UHRF protein family in epigenetics, development, and carcinogenesis

Unoki, Motoko; Sasaki, Hidetada

doi:10.2183/pjab.98.021

Cited by 19 publications

(21 citation statements)

References 129 publications

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“…S4C); UHRF2, which encodes an E3 ubiquitin ligase involved in the maintenance of DNA methylation and has been previously shown to play a role in the intranuclear degradation of polyglutamine aggregates (Fig. 1D) [63][64][65][66][67][68]; and ADARB1, which encodes an adenosine deaminase that catalyzes the conversion of adenosine to inosine in double-stranded RNAs and has been previously shown to display pathology in ALS patients (Fig. S10A) [69,70].…”

Section: Resultsmentioning

confidence: 99%

“…Between exon 9 and 10 Encodes the calcium voltage-gated channel auxiliary subunit beta 2 [64] Brugada syndrome [81] UHRF2 Between exon 4 and 5 Encodes the ubiquitin-like, containing PHD and RING finger domains 2 protein; involved in DNA demethylation and plays a role in the clearance of intranuclear polyglutamine aggregates [66][67][68] Huntington's disease and polyglutamine neurodegenerative diseases [68] ADARB1…”

Section: Cacnb2mentioning

confidence: 99%

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MATR3 pathogenic variants differentially impair its cryptic splicing repression function

Khan,

Chen,

Dias

et al. 2024

FEBS Letters

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Matrin‐3 (MATR3) is an RNA‐binding protein implicated in neurodegenerative and neurodevelopmental diseases. However, little is known regarding the role of MATR3 in cryptic splicing within the context of functional genes and how disease‐associated variants impact this function. We show that loss of MATR3 leads to cryptic exon inclusion in many transcripts. We reveal that ALS‐linked S85C pathogenic variant reduces MATR3 solubility but does not impair RNA binding. In parallel, we report a novel neurodevelopmental disease‐associated M548T variant, located in the RRM2 domain, which reduces protein solubility and impairs RNA binding and cryptic splicing repression functions of MATR3. Altogether, our research identifies cryptic events within functional genes and demonstrates how disease‐associated variants impact MATR3 cryptic splicing repression function.

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Section: Resultsmentioning

confidence: 99%

Section: Cacnb2mentioning

confidence: 99%

MATR3 pathogenic variants differentially impair its cryptic splicing repression function

Khan,

Chen,

Dias

et al. 2024

FEBS Letters

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“…18,20,27 Interestingly, honeybees have UHRF1 protein. 28 The primary amino-acid sequence of honeybee (Apis Mellifera) UHRF1 has been reported (Genbank accession number NP_001229385.1. 77 The fatty acid called 10-Hydroxy-2-decenoic acid (10HDA), the active ingredient in royal jelly inhibits the histone deacetylase HDAC3 through a mechanism involving the high content of zinc in royal jelly.…”

Section: The Epigenetic Integrator Uhrf1 In Honeybeesmentioning

confidence: 99%

Epigenetics Mechanisms of Honeybees: Secrets of Royal Jelly

Alhosin

2023

Genet Epigenet

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Early diets in honeybees have effects on epigenome with consequences on their phenotype. Depending on the early larval diet, either royal jelly (RJ) or royal worker, 2 different female castes are generated from identical genomes, a long-lived queen with fully developed ovaries and a short-lived functionally sterile worker. To generate these prominent physiological and morphological differences between queen and worker, honeybees utilize epigenetic mechanisms which are controlled by nutritional input. These mechanisms include DNA methylation and histone post-translational modifications, mainly histone acetylation. In honeybee larvae, DNA methylation and histone acetylation may be differentially altered by RJ. This diet has biologically active ingredients with inhibitory effects on the de novo methyltransferase DNMT3A or the histone deacetylase 3 HDAC3 to create and maintain the epigenetic state necessary for developing larvae to generate a queen. DNMT and HDAC enzymes work together to induce the formation of a compacted chromatin structure, repressing transcription. Such dialog could be coordinated by their association with other epigenetic factors including the ubiquitin-like containing plant homeodomain (PHD) and really interesting new gene (RING) ﬁnger domains 1 (UHRF1). Through its multiple functional domains, UHRF1 acts as an epigenetic reader of both DNA methylation patterns and histone marks. The present review discusses the epigenetic regulation of honeybee’s chromatin and how the early diets in honeybees can affect the DNA/histone modifying types of machinery that are necessary to stimulate the larvae to turn into either queen or worker. The review also looks at future directions in epigenetics mechanisms of honeybees, mainly the potential role of UHRF1 in these mechanisms.

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“…UHRF1 (Ubiquitin-like with PHD and RING Finger domains 1) is a member of the UHRF protein family [ 1 ]. UHRF1 is an epigenetic coordinator bridging DNA methylation and histone modifications, and has been involved in the regulation of a series of biological functions [ 2 ], such as DNA replication, DNA methylation, and DNA damage repair.…”

Section: Introductionmentioning

confidence: 99%

Roles of post-translational modifications of UHRF1 in cancer

Gu,

Fu,

2024

Epigenetics & Chromatin

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UHRF1 as a member of RING-finger type E3 ubiquitin ligases family, is an epigenetic regulator with five structural domains. It has been involved in the regulation of a series of biological functions, such as DNA replication, DNA methylation, and DNA damage repair. Additionally, aberrant overexpression of UHRF1 has been observed in over ten cancer types, indicating that UHRF1 is a typical oncogene. The overexpression of UHRF1 repressed the transcription of such tumor-suppressor genes as CDKN2A, BRCA1, and CDH1 through DNMT1-mediated DNA methylation. In addition to the upstream transcription factors regulating gene transcription, post-translational modifications (PTMs) also contribute to abnormal overexpression of UHRF1 in cancerous tissues. The types of PTM include phosphorylation, acetylation, methylationand ubiquitination, which regulate protein stability, histone methyltransferase activity, intracellular localization and the interaction with binding partners. Recently, several novel PTM types of UHRF1 have been reported, but the detailed mechanisms remain unclear. This comprehensive review summarized the types of UHRF1 PTMs, as well as their biological functions. A deep understanding of these crucial mechanisms of UHRF1 is pivotal for the development of novel UHRF1-targeted anti-cancer therapeutic strategies in the future.

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The UHRF protein family in epigenetics, development, and carcinogenesis

Cited by 19 publications

References 129 publications

MATR3 pathogenic variants differentially impair its cryptic splicing repression function

MATR3 pathogenic variants differentially impair its cryptic splicing repression function

Epigenetics Mechanisms of Honeybees: Secrets of Royal Jelly

Roles of post-translational modifications of UHRF1 in cancer

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