InteractiveFly: GeneBrief

Age-related lipid regulator: Biological Overview | References

While disorders in lipid metabolism have been associated with aging and age-related diseases, how lipid metabolism is regulated during aging is poorly understood. This study characterize the Drosophila endoribonuclease CG2145, an ortholog of mammalian EndoU that this study named Age-related lipid regulator (Arlr), as a regulator of lipid homeostasis during aging. In adult adipose tissues, arlr is necessary for maintenance of lipid storage in lipid droplets (LDs) as flies age, a phenotype that can be rescued by either high-fat or high-glucose diet. Interestingly, RNA-seq of arlr mutant adipose tissues and RIP-seq suggest that arlraffects lipid metabolism through the degradation of the mRNAs of lipolysis genes - a model further supported by the observation that knockdown of Lsd-1, regucalcin, yip2 (Acetyl-CoA acyltransferase) or CG5162, which encode genes involved in lipolysis, rescue the LD defects of arlr mutants. In addition, DendoU as a functional paralog of arlr was characterize, and human ENDOU was able to rescue arlr mutants. Altogether, this study reveals a role of ENDOU-like endonucleases as negative regulator of lipolysis (Sun, 2023).

Lipid droplets (LDs) are highly dynamic organelles that contain a core of neutral lipids including triacylglycerols (TAGs) and cholesteryl esters, which are surrounded by a phospholipid monolayer. While mostly found in the adipose tissue, LDs are also present in other cells including hepatocytes, enterocytes, macrophages, and adrenocortical cells to store excess lipids. These spherical organelles are regulated by LD-associated proteins which regulate LD biogenesis and degradation, and that play a crucial role in maintaining lipid homeostasis and energy supply (Sun, 2023).

LDs originate from the bilayer endoplasmic reticulum (ER) where the curvature of ER tubules (smooth ER) catalyzes the nucleation of neutral lipids into lenses leading to nascent LD buds. During de novo synthesis, LD size is regulated by Seipin and the Fat Storage-inducing Transmembrane (FIT) proteins, which are associated with lens formation and budding. In addition, LD growth is regulated by TAG synthesis enzymes (e.g., GPAT4, AGPAT3, DGAT1, and DGAT2), which relocalize from the ER to the LD surface14. An alternative mechanism of LD growth is the fusion of existing small LDs by either coalescence or lipid exchange (Sun, 2023).

LD degradation is mediated by lipolysis and lipophagy pathways. During lipolysis, TAG hydrolysis is initiated by adipose triglyceride lipase (ATGL), followed by hormone-sensitive lipase (HSL) that hydrolyzes diacylglycerol (DAG) and monoacylglycerol lipase (MGL) that hydrolyzes monoacylglycerol (MAG), releasing free fatty acids for further degradation through mitochondrial or peroxisomal β-oxidation to generate ATP. LDs can also be degraded through autophagy/lipophagy whereby the whole LD is sequestered by autophagosomes, which is then delivered to lysosomes where it is degraded by lipases. The lipolysis pathway prefers to hydrolyze larger-sized LDs and produces small LDs, whereas the lipophagy machinery can only engulf small LDs, inhibition of which results in accumulation of small LDs22 (Sun, 2023).

A number of key proteins have been identified as regulators of the size and number of LDs, such as cell death-inducing DFFA-like effector c (CIDEC) proteins and perilipins. In adipocyte cell lines, FSP27/CIDEC is enriched at LD-LD contact sites and mediates directional transfer of lipids from smaller to larger LDs. Located at the surface of LDs, PLIN1, the best characterized LD perilipin (PLIN), plays a dual role in lipid metabolism, limiting lipase access to stored TAGs in the fed state or facilitating in the fast state hormonally-stimulated lipolysis. Phosphorylated PLIN1 serves as a scaffold for lipases to drive lipolysis, and for proteins such as FSP27 to regulate LD growth. Consistent with this, in Drosophila the lipid storage droplet protein 1 (Lsd-1/PLIN1) stimulates lipolysis by recruiting Hormone-sensitive lipase (HSL) to the LD surface while Lsd-2/PLIN2 promotes lipogenesis by antagonizing ATGL/Brummer (Bmm) activity (Sun, 2023).

Understanding LD dynamics and metabolism is of great significance for lipid metabolism-associated disorders, aging, and lifespan. For example, during aging a change in overall lipid metabolism has been observed, usually leading to lipid accumulation in the adipose tissue and ectopic accumulation in non-adipose tissues, which increases the risk of developing metabolic diseases. Other studies have demonstrated that the activity of HSL is reduced in the aged adipose tissue, which is consistent with lipid changes in aging organisms. Further, genetic studies on enzymes that regulate biosynthesis and mobilization of neutral lipids, such as diacylglycerol acyltransferase 1 (DGAT1) in mice, or ATGL and diacylglycerol lipase (DAGL) in C. elegans and Drosophila, support the association of increased lipolysis with longevity. On the other hand, increased TAG levels with extended lifespan are also observed along with increased fat synthesis and breakdown, indicating that increased lipid mobilization helps extend lifespan. In addition, lipid metabolism is regulated by highly conserved pro-longevity signaling pathways, such as insulin/insulin-like growth factor signaling (IIS) and mechanistic target of rapamycin (mTOR) signaling, as well as by dietary restriction. These pathways extend lifespan, usually through activation of lipolysis via upregulation of lipases, desaturation of fatty acids, and lipophagy. In particular, the transcription factor FoxO, which is inhibited by IIS and activated by starvation, stimulates ATGL/Bmm and other lipases through transcription or indirect modifications to promote lipolysis4. Despite these studies, how LDs are regulated during aging is poorly understood (Sun, 2023).

This study has identified the endoribonuclease (EndoU) Arlr as an age-related lipid regulator. The EndoU family proteins have a conserved RNA binding domain that cleaves single-stranded RNA harboring U-rich sequences. High expression levels of Arlr during aging are essential for lipid accumulation in LDs, and loss of arlr results in rapid lipid consumption. Mechanistically, this study shows that Arlr controls the homeostasis of LDs by affecting the stability of mRNAs encoding proteins involved in lipolysis. In addition, it was demonstrated that both a paralog of Arlr, DendoU, and human ENDOU also act as negative regulators of lipolysis, as they can rescue arlr mutants (Sun, 2023).

This study reports that high expression of the endonuclease Arlr during aging is essential for lipid accumulation and that in the absence of Arlr activity lipid storage in LDs in adult adipose tissues is affected due to an increase in lipolysis. Arlr binds to the mRNAs of a number of lipolytic genes and negatively regulates their expression and the endonuclease domain of Arlr is necessary to rescue arlr mutants. Altogether, it is proposed that the endoribonuclease Arlr is required to maintain lipid homeostasis by downregulating lipolytic genes (Sun, 2023).

Previous studies have implicated the EndoU protein family in lipid metabolism by affecting mRNA levels. The nematode homolog ENDU-2 protects germline immortality via downregulation of genes involved in lipid metabolism. However, in contrast to the current findings, the lipid content is increased in ENDU-2 mutants. As the specific targets of ENDU-2 have not yet been characterized, further studies will be needed to reconcile these observations. In addition, overexpression of the zebrafish or human ENDOU increases human CHOP mRNA translation via cleavage of the upstream open reading frames (uORFs), which negatively affects translation of C/EBP homologous protein (CHOP). As a transcription factor, CHOP is upregulated by lipid accumulation-induced ER stress and interacts with FoxO to promote hepatic lipogenesis through activation of peroxisome proliferator-activated receptor γ (PPARgamma;) expression. In addition, lipids are reduced in CHOP knockdown cell lines64. However, severe impairment of ER activates CHOP to induce lipoapoptosis, thus inhibiting adipogenesis, probably through specific target genes67. Despite these studies, the role of EndoU proteins in lipid metabolism has remained largely unknown (Sun, 2023).

EndoU proteins, which contain RNA binding domains, cleave single-stranded RNA harboring U-rich sequences. This study found that a number of lipolytic genes are negatively regulated by Arlr via its binding to target mRNAs and that the EndoU domain is required for Arlr activity. Strikingly, knockdown of four lipolytic genes, Lsd-1, CG5162, yip2, and regucalcin, rescues the LD defects in arlr mutants Lsd-1 proteins form a scaffold on the surface of LDs and recruit lipases such as HSL to stimulate lipolysis. Lsd-1 is exclusively expressed in fat bodies and Lsd-1 mutants display giant LDs both in larvae and adult flies and exhibit adult-onset obesity. In contrast, overexpression of Lsd-1 in the fat body results in small LDs. Interestingly, AKH/Glucagon signaling phosphorylates Lsd-1 to stimulate lipolysis in adult flies. As the AKH receptor is normally expressed in arlr mutants, it will be interesting to test whether Arlr antagonizes AKH. In addition, as cytoplasmic lipase-driven lipolysis acts on large LDs, only large-sized medial LDs (mLDs) are regulated by Arlr, but not small peripheral LDs (pLDs). This is consistent with the mechanism that mLDs rely on Lsd-1, whereas pLDs are regulated by Lsd-2 and the LD-PM (plasma membrane) contact protein Snazarus. Among the other targets, CG5162 mRNA levels have been previously reported to increase in response to acute exercise which leads to a significant reduction in LD size. This is consistent with its role in lipolysis. Interestingly, two other major lipases, HSL and Bmm, are not transcriptionally regulated by Arlr. Further characterization of the epistatic relationships between Bmm, HSL and Arlr will be of interest. Another target, Yip2, is a fasting-inducible gene that acts in the catalysis of fatty acid oxidation. Finally, Regucalcin/SMP30 transcriptionally represses the adipokines leptin and adiponectin, but how Regucalcin/SMP30 regulates lipid metabolism is not clear. Altogether, it is speculated that EndoU family proteins influence the synthesis of lipolytic proteins by releasing mRNAs from the ER membrane. When Arlr is lost, the function of mRNA degradation is impaired, resulting in accelerated lipolysis of large medial LDs, ultimately leading to fast lipid consumption in aging flies (Sun, 2023).

The two fly paralogs of EndoU, Arlr and DendoU, share similar functions during lipid metabolism. Mutations of either gene lead to reduced fat content. However, while the number of LDs in dendoU-knockdown flies is reduced, small LD size is the major defect in arlr mutants in aging flies. In vitro RNA processing assays indicate that DendoU preferentially cleaves at oligo(U), whereas Arlr preferentially cleaves between A and C nucleotides and has less preference for oligo(U)50. Moreover, although some residues that are essential for RNA binding and RNA cleavage are conserved in both Arlr and DendoU, others located at the N terminal variable region that are essential for RNA binding are less conserved, suggesting that DendoU and Arlr have both common and distinct molecular targets. Despite these differences, expression of either gene is sufficient to rescue the LD defects in each mutant. Further, a short period of starvation induces moderate expression of arlr and downregulation of dendoU in fat bodies, indicating a compensatory regulation of these two EndoU genes to keep the balance of lipid metabolism. In addition, like dendoU, expressing human ENDOU can compensate for loss of arlr. Taken together, these findings reveal a conserved role of EndoU family proteins in lipid metabolism and that these proteins may function through distinct targets but have complementary roles in lipid accumulation (Sun, 2023).

Interestingly, EndoU proteins in most species contain a signal peptide at the N terminus and can be secreted. Previously, it was reported that knockdown of arlrin the fat body was associated with poor climbing ability consistent with defects in muscle activity and Ubiquitin protein aggregates in muscles55. In addition, Arlr could be detected at the surface of thoracic muscles suggesting that fat body derived Arlr directly affect muscle activity. Further, in C. elegans, secreted EndoU from the soma has been found to protect germline immortality61. Intriguingly, overexpressing dendoU, which has no signal peptide sequence, leads to enlarged LDs, similar to arlrΔSP (signal peptide-deprived Arlr). However, overexpressing full-length arlror human ENDOU show normal LDs (Figs. 2, 7), which is likely due to its secretory capacity. Further studies will be required to characterize the exact role of secreted EndoU proteins (Sun, 2023).

In aging flies, the highest DEGs are in the fat body and several adipose cell types, highlighting that major changes occur in fat cells during aging. arlr is highly expressed during adult stages and snRNAseq analysis of the FCA and AFCA data sets shows that the expression of Arlr is increased in aging fat cells. Consistent with the high levels of Arlr, expression of the target senescence marker gene regucalcin/SMP30 decreases with age in rats, indicating that Arlr could be a marker of aging. Arlr attenuates lipolytic gene expression, resulting in lipid homeostasis in aging flies. Aging-associated reduction of lipolysis is mediated by inhibition of lipolytic pathways, such as the decrease of HSL and ATGL with age. Further, promoting lipolysis by genetic manipulations and dietary restriction (DR) is considered to be associated with lifespan extension. Upon DR, flies shift their metabolism toward increasing fatty-acid synthesis and breakdown, and disruption of lipid synthesis or oxidation inhibits lifespan extension upon DR, indicating that lipid homeostasis is essential for lifespan extension42. In arlr mutants, lipid consumption is severely accelerated, indicating a disruption of lipid homeostasis, thus lifespan is reduced under standard food and starvation conditions. Excessive nutrition replenishes the lipid content and rescues the short lifespan of arlrmutants. Thus, Arlr is essential for longevity by promoting the balance of lipid metabolism via lipolytic regulation (Sun, 2023).

EndoU family of endonucleases have been implicated in many processes, including as a tumor biomarker in human beings, immune response in mice, ER morphology in Xenopus, neurodegeneration in Drosophila, cold tolerance, nucleotide metabolism, lifespan and germline immortality in C. elegans, and viral replication and pathogenicity. The current findings reveal another role of EndoU family proteins in lipolysis and provide mechanistic insights for such a specific function. Understanding of EndoU in lipid metabolism may provide insights for the treatment of lipid metabolism-associated diseases and promotes healthy aging (Sun, 2023).

Coronavirus endoribonuclease antagonizes ZBP1-mediated necroptosis and delays multiple cell death pathways

Identifying conserved mechanisms used by viruses to delay host innate responses can reveal potential targets for antiviral therapeutics. This study investigated coronavirus nonstructural protein 15 (nsp15), which encodes a highly conserved endoribonuclease (EndoU). EndoU functions as an immune antagonist by limiting the accumulation of viral replication intermediates that would otherwise be sensed by the host. Despite being a promising antiviral target, it has been difficult to develop small-molecule inhibitors that target the EndoU active site. nsp15 mutants of the coronaviruses severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and mouse hepatitis virus (MHV)-A59 were generated, and conserved residues were generated within the amino-terminal domain that are required for EndoU activity. Loss of EndoU activity caused the activation of host sensors, which limited viral replication in interferon-responsive cells and attenuated disease in MHV-infected mice. Using transcriptional profiling, MHV EndoU mutant viruses were found to upregulate multiple host sensors, including Z-form nucleic acid-binding protein 1 (ZBP1). nsp15 mutants induced early, robust ZBP1-mediated necroptosis. EndoU mutant viruses also induced ZBP1-independent apoptosis and pyroptosis pathways, causing early, robust cell death that limits virus replication and pathogenesis. Overall, this study documents the importance of the amino-terminal domain for EndoU function. The importance of nsp15/EndoU activity for evading host sensors, delaying cell death, and promoting pathogenesis is highlighted (Evdokimova, 2025).

Molecular basis for the calcium-dependent activation of the ribonuclease EndoU

Ribonucleases (RNases) are ubiquitous enzymes that process or degrade RNA, essential for cellular functions and immune responses. The EndoU-like superfamily includes endoribonucleases conserved across bacteria, eukaryotes, and certain viruses, with an ancient evolutionary link to the ribonuclease A-like superfamily. Both bacterial EndoU and animal RNase A share a similar fold and function independently of cofactors. In contrast, the eukaryotic EndoU catalytic domain requires divalent metal ions for catalysis, possibly due to an N-terminal extension near the catalytic core. In this study, we use biophysical and computational techniques along with in vitro assays to investigate the calcium-dependent activation of human EndoU. We determine the crystal structure of EndoU bound to calcium and find that calcium binding remote from the catalytic triad triggers water-mediated intramolecular signaling and structural changes, activating the enzyme through allostery. Calcium binding involves residues from both the catalytic core and the N-terminal extension, indicating that the N-terminal extension interacts with the catalytic core to modulate activity in response to calcium. These findings suggest that similar mechanisms may be present across all eukaryotic EndoUs, highlighting a unique evolutionary adaptation that connects endoribonuclease activity to cellular signaling in eukaryotes (Malard, 2025).

Reprogramming of the transcriptome after heat stress mediates heat hormesis in Caenorhabditis elegans

Transient stress experiences not only trigger acute stress responses, but can also have long-lasting effects on cellular functions. In Caenorhabditis elegans, a brief exposure to heat shock during early adulthood extends lifespan and improves stress resistance, a phenomenon known as heat hormesis. This study investigated the prolonged effect of hormetic heat stress on the transcriptome of worms and found that the canonical heat shock response is followed by a profound transcriptional reprogramming in the post-stress period. This reprogramming relies on the endoribonuclease ENDU-2 but not the heat shock factor 1. ENDU-2 co-localizes with chromatin and interacts with RNA polymerase II, enabling specific regulation of transcription after the stress period. Failure to activate the post-stress response does not affect the resistance of animals to heat shock but eliminates the beneficial effects of hormetic heat stress. In summary, this work discovers that the RNA-binding protein ENDU-2 mediates the long-term impacts of transient heat stress via reprogramming transcriptome after stress exposure (Xu, 2023).

The Upstream 1350~1250 Nucleotide Sequences of the Human ENDOU-1 Gene Contain Critical Cis-Elements Responsible for Upregulating Its Transcription during ER Stress

ENDOU-1 encodes an endoribonuclease that overcomes the inhibitory upstream open reading frame (uORF)-trap at 5'-untranslated region (UTR) of the CHOP transcript, allowing the downstream coding sequence of CHOP be translated during endoplasmic reticulum (ER) stress. However, transcriptional control of ENDOU-1 remains enigmatic. To address this, we cloned an upstream 2.1 kb (-2055~+77 bp) of human ENDOU-1 (pE2.1p) fused with reporter luciferase (luc) cDNA. The promoter strength driven by pE2.1p was significantly upregulated in both pE2.1p-transfected cells and pE2.1p-injected zebrafish embryos treated with stress inducers. Comparing the luc activities driven by pE2.1p and -1125~+77 (pE1.2p) segments, we revealed that cis-elements located at the -2055~-1125 segment might play a critical role in ENDOU-1 upregulation during ER stress. Since bioinformatics analysis predicted many cis-elements clustered at the -1850~-1250, we further deconstructed this segment to generate pE2.1p-based derivatives lacking -1850~-1750, -1749~-1650, -1649~-1486, -1485~-1350 or -1350~-1250 segments. Quantification of promoter activities driven by these five internal deletion plasmids suggested a repressor binding element within the -1649~-1486 and an activator binding element within the -1350~-1250. Since luc activities driven by the -1649~-1486 were not significantly different between normal and stress conditions, we herein propose that the stress-inducible activator bound at the -1350~-1250 segment makes a major contribution to the increased expression of human ENDOU-1 upon ER stresses (Lee, 2023).

Poly(U)-specific endoribonuclease ENDOU promotes translation of human CHOP mRNA by releasing uORF element-mediated inhibition

Upstream open reading frames (uORFs) are known to negatively affect translation of the downstream ORF. The regulatory proteins involved in relieving this inhibition are however poorly characterized. In response to cellular stress, eIF2alpha phosphorylation leads to an inhibition of global protein synthesis, while translation of specific factors such as CHOP is induced. This study analyzed a 105-nt inhibitory uORF in the transcript of human CHOP (huORF(chop)) and found that overexpression of the zebrafish or human ENDOU poly(U)-endoribonuclease (Endouc or ENDOU-1, respectively) increases CHOP mRNA translation also in the absence of stress. Endouc/ENDOU-1 was found to binds and cleaves the huORF(chop) transcript at position 80G-81U, which induces CHOP translation independently of phosphorylated eIF2alpha. However, both ENDOU and phospho-eIF2alpha are nonetheless required for maximal translation of CHOP mRNA. Increased levels of ENDOU shift a huORF(chop) reporter as well as endogenous CHOP transcripts from the monosome to polysome fraction, indicating an increase in translation. Furthermore, we found that the uncapped truncated huORF(chop) -69-105-nt transcript contains an internal ribosome entry site (IRES), facilitating translation of the cleaved transcript. Therefore, we propose a model where ENDOU-mediated transcript cleavage positively regulates CHOP translation resulting in increased CHOP protein levels upon stress. Specifically, CHOP transcript cleavage changes the configuration of huORF(chop) thereby releasing its inhibition and allowing the stalled ribosomes to resume translation of the downstream ORF (Lee, 2021).

Coronavirus endoribonuclease targets viral polyuridine sequences to evade activating host sensors

Coronaviruses (CoVs) are positive-sense RNA viruses that can emerge from endemic reservoirs and infect zoonotically, causing significant morbidity and mortality. CoVs encode an endoribonuclease designated EndoU that facilitates evasion of host pattern recognition receptor MDA5, but the target of EndoU activity was not known. This study reports that EndoU cleaves the 5'-polyuridines from negative-sense viral RNA, termed PUN RNA, which is the product of polyA-templated RNA synthesis. Using a virus containing an EndoU catalytic-inactive mutation, a higher abundance of PUN RNA was found in the cytoplasm compared to wild-type-infected cells. Furthermore, transfecting PUN RNA into cells stimulates a robust, MDA5-dependent interferon response, and that removal of the polyuridine extension on the RNA dampens the response. Overall, the results of this study reveal the PUN RNA to be a CoV MDA5-dependent pathogen-associated molecular pattern (PAMP). This study also establish a mechanism for EndoU activity to cleave and limit the accumulation of this PAMP. Since EndoU activity is highly conserved in all CoVs, inhibiting this activity may serve as an approach for therapeutic interventions against existing and emerging CoV infections (Hackbart, 2020).

EndoU is a novel regulator of AICD during peripheral B cell selection

Balanced transmembrane signals maintain a competent peripheral B cell pool limited in self-reactive B cells that may produce pathogenic autoantibodies. To identify molecules regulating peripheral B cell survival and tolerance to self-antigens (Ags), a gene modifier screen was performed with B cells from CD22-deficient C57BL/6 (CD22(-/-[B6])) mice that undergo activation-induced cell death (AICD) and fail to up-regulate c-Myc expression after B cell Ag receptor ligation. Likewise, lysozyme auto-Ag-specific B cells in Ig(Tg) hen egg lysozyme (HEL) transgenic mice inhabit the spleen but undergo AICD after auto-Ag encounter. This gene modifier screen identified EndoU, a single-stranded RNA-binding protein of ancient origin, as a major regulator of B cell survival in both models. EndoU gene disruption prevents AICD and normalizes c-Myc expression. These findings reveal that EndoU is a critical regulator of an unexpected and novel RNA-dependent pathway controlling peripheral B cell survival and Ag responsiveness that may contribute to peripheral B cell tolerance (Poe, 2014).

Search PubMed for articles about Drosophila Arir

Evdokimova, M., Feng, S., Caobi, A., Moreira, F. R., Jones, D., Alysandratos, K. D., Tully, E. S., Kotton, D. N., Boyd, D. F., Banach, B. S., Kirchdoerfer, R. N., Saeed, M., Baker, S. C. (2025). Coronavirus endoribonuclease antagonizes ZBP1-mediated necroptosis and delays multiple cell death pathways. Proc Natl Acad Sci U S A, 122(10):e2419620122 PubMed ID: 40035769

Hackbart, M., Deng, X., Baker, S. C. (2020). Coronavirus endoribonuclease targets viral polyuridine sequences to evade activating host sensors. Proc Natl Acad Sci U S A, 117(14):8094-8103 PubMed ID: 32198201

Lee, H. C., Fu, C. Y., Lin, C. Y., Hu, J. R., Huang, T. Y., Lo, K. Y., Tsai, H. Y., Sheu, J. C., Tsai, H. J. (2021). Poly(U)-specific endoribonuclease ENDOU promotes translation of human CHOP mRNA by releasing uORF element-mediated inhibition. EMBO J, 40(11):e104123 PubMed ID: 33511665

Lee, H. C., Chao, H. T., Lee, S. Y., Lin, C. Y., Tsai, H. J. (2023). The Upstream 1350~1250 Nucleotide Sequences of the Human ENDOU-1 Gene Contain Critical Cis-Elements Responsible for Upregulating Its Transcription during ER Stress. Int J Mol Sci, 24(24) PubMed ID: 38139221

Malard, F., Dias, K., Baudy, M., Thore, S., Vialet, B., Barthelemy, P., Fribourg, S., Karginov, F. V., Campagne, S. (2025). Molecular basis for the calcium-dependent activation of the ribonuclease EndoU. Nat Commun, 16(1):3110 PubMed ID: 40169637

Poe, J. C., Kountikov, E. I., Lykken, J. M., Natarajan, A., Marchuk, D. A., Tedder, T. F. (2014). EndoU is a novel regulator of AICD during peripheral B cell selection. J Exp Med, 211(1):57-69 PubMed ID: 24344237

Sun, X., Shen, J., Perrimon, N., Kong, X., Wang, D. (2023). The endoribonuclease arlr is required to maintain lipid homeostasis by downregulating lipolytic genes during aging. Nat Commun, 14(1):6254 PubMed ID: 37803019

Xu, F., Li, R., von Gromoff, E. D., Drepper, F., Knapp, B., Warscheid, B., Baumeister, R., Qi, W. (2023). Reprogramming of the transcriptome after heat stress mediates heat hormesis in Caenorhabditis elegans. Nat Commun, 14(1):4176 PubMed ID: 37443152

date revised: 5 August 2025

Home page: The Interactive Fly © 2025 Thomas Brody, Ph.D.