LOTUS domain protein MARF1 binds CCR4-NOT deadenylase complex to post-transcriptionally regulate gene expression in oocytes

Zhu, Li; Kandasamy, Suresh K.; Liao, Susan E.; Fukunaga, Ryuya

doi:10.1038/s41467-018-06404-w

Cited by 33 publications

(44 citation statements)

References 59 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…nos may not be the only target of dMarf1; other mRNAs such as tra2 and abo can also be targeted by dMarf1, although the biological significance of these interactions remains unclear. Zhu et al have recently reported that dMarf1 can bind to cyclin A mRNA via its RRM domain [8]. However, our RNA-IP analysis did not detect cyclin A in the dMarf1-bound mRNA fraction (S4 Table).…”

Section: Plos Onecontrasting

confidence: 56%

“…The C-terminal region of the MARF1 family members is highly conserved among higher animals, except insects (S3 and S4 Figs), despite not forming any secondary structure. The Cterminal region of human MARF1 has been shown to directly interact with the decapping complex component Ge-1 [21]; however, this interaction was not observed in Drosophila [8]. Moreover, the C-terminal region of the MARF1 family members is conserved among different insect species, but different from that of higher animals (S4 Fig), indicating that it may bind to a unique partner in insects.…”

Section: Plos Onementioning

confidence: 98%

“…During our study, Fukunaga's group at Johns Hopkins reported a characterization of dMarf1 [8]; dMarf1 was required for the meiosis completion and interacted with CCR4-NOT deadenylase. They also found that cyclin A was one of the targets of the dMarf1/CCR4-NOT function and proposed the mechanism of the temporal regulation of cyclin A reduction during late oogenesis.…”

Section: Introductionmentioning

confidence: 94%

“…elusive [8]. In addition to these two domains, the MARF1 family members contain one or two RRM domains.…”

Section: Plos Onementioning

confidence: 99%

See 3 more Smart Citations

Drosophila MARF1 ensures proper oocyte maturation by regulating nanos expression

Kawaguchi¹,

Ueki²,

Kai³

2020

PLoS ONE

View full text Add to dashboard Cite

Meiosis and oocyte maturation are tightly regulated processes. The meiosis arrest female 1 (MARF1) gene is essential for meiotic progression in animals; however, its detailed function remains unclear. In this study, we examined the molecular mechanism of dMarf1, a Drosophila homolog of MARF1 encoding an OST and RNA Recognition Motif (RRM)-containing protein for meiotic progression and oocyte maturation. Although oogenesis progressed in females carrying a dMarf1 loss-of-function allele, the dMarf1 mutant oocytes were found to contain arrested meiotic spindles or disrupted microtubule structures, indicating that the transition from meiosis I to II was compromised in these oocytes. The expression of the full-length dMarf1 transgene, but none of the variants lacking the OST and RRM motifs or the 47 conserved C-terminal residues among insect groups, rescued the meiotic defect in dMarf1 mutant oocytes. Our results indicate that these conserved residues are important for dMarf1 function. Immunoprecipitation of Myc-dMarf1 revealed that several mRNAs are bound to dMarf1. Of those, the protein expression of nanos (nos), but not its mRNA, was affected in the absence of dMarf1. In the control, the expression of Nos protein became downregulated during the late stages of oogenesis, while it remained high in dMarf1 mutant oocytes. We propose that dMarf1 translationally represses nos by binding to its mRNA. Furthermore, the downregulation of Nos induces cycB expression, which in turn activates the CycB/Cdk1 complex at the onset of oocyte maturation.

show abstract

Section: Plos Onecontrasting

confidence: 56%

Section: Plos Onementioning

confidence: 98%

Section: Introductionmentioning

confidence: 94%

“…elusive [8]. In addition to these two domains, the MARF1 family members contain one or two RRM domains.…”

Section: Plos Onementioning

confidence: 99%

See 2 more Smart Citations

Drosophila MARF1 ensures proper oocyte maturation by regulating nanos expression

Kawaguchi¹,

Ueki²,

Kai³

2020

PLoS ONE

View full text Add to dashboard Cite

show abstract

“…True NYN proteins also include Limkain enzymes, such as MARF1 in animals and MNU1 and MNU2 in plants (Table ). MARF1 is localized in P‐bodies where it interacts with components of the decapping complex and in Drosophila can recruit the CCR4‐NOT deadenylase complex . While MARF1 enzymes always occur in animals, their overall structure varies.…”

Section: Introductionmentioning

confidence: 99%

Involvement of PIN‐like domain nucleases in tRNA processing and translation regulation

2019

View full text Add to dashboard Cite

Transfer RNAs require essential maturation steps to become functional. Among them, RNase P removes 5′ leader sequences of pre‐tRNAs. Although RNase P was long thought to occur universally as ribonucleoproteins, different types of protein‐only RNase P enzymes were discovered in both eukaryotes and prokaryotes. Interestingly, all these enzymes belong to the super‐group of PilT N‐terminal‐like nucleases (PIN)‐like ribonucleases. This wide family of enzymes can be subdivided into major subgroups. Here, we review recent studies at both functional and mechanistic levels on three PIN‐like ribonucleases groups containing enzymes connected to tRNA maturation and/or translation regulation. The evolutive distribution of these proteins containing PIN‐like domains as well as their organization and fusion with various functional domains is discussed and put in perspective with the diversity of functions they acquired during evolution, for the maturation and homeostasis of tRNA and a wider array of RNA substrates. © 2019 IUBMB Life, 2019 © 2019 IUBMB Life, 71(8):1117–1125, 2019

show abstract

Diverse functions of deadenylases in DNA damage response and genomic integrity

Yan

2020

WIREs RNA

View full text Add to dashboard Cite

DNA damage response (DDR) is a coordinated network of diverse cellular processes including the detection, signaling, and repair of DNA lesions, the adjustment of metabolic network and cell fate determination. To deal with the unavoidable DNA damage caused by either endogenous or exogenous stresses, the cells need to reshape the gene expression profile to allow efficient transcription and translation of DDR‐responsive messenger RNAs (mRNAs) and to repress the nonessential mRNAs. A predominant method to adjust RNA fate is achieved by modulating the 3′‐end oligo(A) or poly(A) length via the opposing actions of polyadenylation and deadenylation. Poly(A)‐specific ribonuclease (PARN) and the carbon catabolite repressor 4 (CCR4)‐Not complex, the major executors of deadenylation, are indispensable to DDR and genomic integrity in eukaryotic cells. PARN modulates cell cycle progression by regulating the stabilities of mRNAs and microRNA (miRNAs) involved in the p53 pathway and contributes to genomic stability by affecting the biogenesis of noncoding RNAs including miRNAs and telomeric RNA. The CCR4‐Not complex is involved in diverse pathways of DDR including transcriptional regulation, signaling pathways, mRNA stabilities, translation regulation, and protein degradation. The RNA targets of deadenylases are tuned by the DDR signaling pathways, while in turn the deadenylases can regulate the levels of DNA damage‐responsive proteins. The mutual feedback between deadenylases and the DDR signaling pathways allows the cells to precisely control DDR by dynamically adjusting the levels of sensors and effectors of the DDR signaling pathways. Here, the diverse functions of deadenylases in DDR are summarized and the underlying mechanisms are proposed according to recent findings. This article is categorized under: RNA Processing > 3' End Processing RNA in Disease and Development > RNA in Disease RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms

show abstract

LOTUS domain protein MARF1 binds CCR4-NOT deadenylase complex to post-transcriptionally regulate gene expression in oocytes

Cited by 33 publications

References 59 publications

Drosophila MARF1 ensures proper oocyte maturation by regulating nanos expression

Drosophila MARF1 ensures proper oocyte maturation by regulating nanos expression

Involvement of PIN‐like domain nucleases in tRNA processing and translation regulation

Diverse functions of deadenylases in DNA damage response and genomic integrity

Contact Info

Product

Resources

About