Insect Biochemistry and Molecular Biology最新文献

{"title":"CSP15 attenuates chlorpyrifos toxicity through sequestration and bioactivation suppression in Nilaparvata lugens","authors":"Mengqing Deng,&nbsp;Xiyue Xu,&nbsp;Zhiming Yang,&nbsp;Kai Lu","doi":"10.1016/j.ibmb.2025.104453","DOIUrl":"10.1016/j.ibmb.2025.104453","url":null,"abstract":"<div><div>The escalating problem of insecticide resistance in agricultural pests highlights the need to identify non-canonical resistance mechanisms. In this study, comparative transcriptional analysis identified five chemosensory protein (CSP) genes significantly overexpressed in a chlorpyrifos (CPF)-resistant strain of <em>Nilaparvata lugens</em>. RNA interference and heterologous expression confirmed their contribution to resistance, with <em>CSP15</em>, exhibiting 42.98-fold overexpression, identified as a key mediator. <em>CSP15</em> knockdown increased CPF susceptibility 1.76-fold, while its bacterial expression raised tolerance 5.47-fold. Competitive fluorescence binding assays showed that CSP15 binds CPF (<em>K</em>_i = 3.32 μM) with higher affinity than its toxic metabolite chlorpyrifos-oxon (CPO; <em>K</em>_i = 6.00 μM). Structural modeling revealed a CPF-binding pocket mediated by Arg84 and Lys118. CPO binding utilized four hydrogen bonds with Lys28; the K28A mutation induced structural rearrangement through neo-formed interactions with Arg84 and Lys118, reducing the binding free energy by −40.95 kcal mol⁻¹. Mutagenesis revealed that R84A/K118A double mutants lost 62.85–64.37 % of CPF-binding capacity, whereas the K28A variant increased CPO affinity by 22.65 %. <em>In vivo</em> metabolic profiling indicated that <em>CSP15</em> knockdown promoted CPF degradation and CPO accumulation, supporting its role in suppressing bioactivation. Yeast two-hybrid assays confirmed a direct interaction between CSP15 and CYP6BD12, the P450 enzyme responsible for CPF bioactivation. Additionally, <em>CSP15</em> expression was regulated by the transcription factor Lim1β through two conserved promoter <em>cis</em>-elements. Together, these findings reveal a novel dual resistance mechanism wherein CSP15 acts synergistically by sequestering CPF and binding CYP6BD12, thereby effectively suppressing bioactivation and identifying promising targets for pest management.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"186 ","pages":"Article 104453"},"PeriodicalIF":3.7,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145577095","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lysosomal acid lipase-1 functions in autophagy occurrence and lipid homeostasis dependent of heat shock protein 83 in insects","authors":"Peng Zeng ,&nbsp;Xiaodong Li ,&nbsp;Xuan Jin ,&nbsp;Qien Zhong ,&nbsp;Fareed Uddin Memon ,&nbsp;Youliang Pan ,&nbsp;Yang Xiao ,&nbsp;Kang Li ,&nbsp;Ling Tian","doi":"10.1016/j.ibmb.2025.104447","DOIUrl":"10.1016/j.ibmb.2025.104447","url":null,"abstract":"<div><div>Lysosomal Acid Lipase (LAL) is the key enzyme responsible for hydrolyzing cholesteryl esters and triglycerides within lysosomes. Its dysfunction is linked to various metabolic disorders in humans. However, its biological functions display tissue-specific heterogeneity, and the roles of its homologs in invertebrates remain largely unexplored. Herein, we demonstrated the lysosomal localization of acid lipase-1 (BmAL1) in <em>Bombyx mori</em> through fluorescent protein observation and Co-immunoprecipitation with the lysosomal membrane glycoprotein BmLAMP1. <em>BmAL1</em> overexpression promoted lysosomal acidification, enhanced autophagy, and reduced lipid droplet (LD) formation after oleic acid or palmitic acid treatment. Conversely, <em>BmAL1</em> knockout or knockdown inhibited lysosomal acidification, autophagic flux, and lipid degradation. Subsequently, immunoprecipitation coupled with LC-MS analysis revealed that the BmAL1-interacting proteins were mainly associated with metabolic and human-disease pathways. Notably, functional disruption of BmAL1-interacting protein BmHSP83/BmHSP90 (heat shock protein) compromised BmAL1-mediated lysosomal acidification, autophagy induction, lipid metabolism, and the physical interaction between BmAL1 and BmLAMP1. These data fill a critical gaps in LAL research in invertebrates, and highlight potential targets for the utilization of beneficial insects and the development of pest control strategies.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"186 ","pages":"Article 104447"},"PeriodicalIF":3.7,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145527177","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Limited association of m6A RNA modification with post-transcriptional regulation during honeybee caste differentiation","authors":"Chen Yang ,&nbsp;Yu Zhu He ,&nbsp;Yu Xiang Wang ,&nbsp;Xing Chao Yan ,&nbsp;Xu Han ,&nbsp;Zhi Jiang Zeng ,&nbsp;Xu Jiang He","doi":"10.1016/j.ibmb.2025.104446","DOIUrl":"10.1016/j.ibmb.2025.104446","url":null,"abstract":"<div><div>Honeybee caste differentiation is a prime example of phenotypic plasticity in eusocial insects and serves as a valuable model for epigenetic studies. Various epigenetic modifications such as non-coding RNAs and histone modifications, have been implicated in caste differentiation. However, the role of some epigenetic modifications such as DNA methylation still remains controversial. Similarly, mRNA m⁶A modification has been suggested to participate in honeybee caste differentiation. Here we used Oxford Nanopore technology to compare m⁶A modifications in 2d, 4d, and 6d queen and worker larvae. Our data indicated that m⁶A modification is unlikely to exert a direct role in the caste differentiation at the developmental stages examed in this study. We identified 363, 1074, and 1000 differentially expressed transcripts (DETs) in 2d, 4d, and 6d queen-worker larval comparisons, respectively, 74 of which were mapped in seven key KEGG pathways (e.g., mTOR, Notch, FoxO, MAPK, Wnt, Hippo, Hedgehog) associated with honeybee caste differentiation. In contrast, only 16, 39, and 11 differentially m⁶A-modified transcripts (m⁶A-DMTs) were found in the 2d, 4d and 6d comparisons, with very few m⁶A-DMTs involved in key pathways for caste differentiation. Notably, no correlation was observed between m⁶A modification levels and transcript expression, including DETs and m⁶A-DMTs. The motifs of m⁶A modifications remained unchanged across all three developmental time points. When the original samples were randomly regrouped, the number of m⁶A-DMTs did not change significantly, but the DETs related to caste differentiation were dramatically altered. Therefore, the functional relevance of m⁶A in honeybee caste differentiation is still under debate and requires more comprehensive studies.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"186 ","pages":"Article 104446"},"PeriodicalIF":3.7,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145522484","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Master genetic switches controlling sexual development in Leptinotarsa decemlineata","authors":"Jiangjie Li ,&nbsp;Yimeng Chen ,&nbsp;Jing Wang,&nbsp;Clauvis NT. Taning,&nbsp;Kristof De Schutter","doi":"10.1016/j.ibmb.2025.104451","DOIUrl":"10.1016/j.ibmb.2025.104451","url":null,"abstract":"<div><div>Sex determination is a fundamental process during early embryonic development that shapes the morphological, physiological, and behavioral sexual dimorphism of an organism. Insects, the most diverse group of animals on earth, have evolved a wide range of sex determination systems. This study investigates the sex determination and differentiation in the Colorado potato beetle (CPB), a species with an X0 sex chromosome system, by identifying key regulatory genes involved in these processes. Our findings reveal that the genes <em>Sex-lethal</em> (<em>Sxl</em>), <em>transformer-2</em> (<em>tra2</em>), <em>doublesex</em> (<em>dsx</em>), and <em>fruitless</em> (<em>fru</em>) are highly conserved and all contribute to fertility. Among them, <em>dsx</em> and <em>tra2</em> emerge as key genetic switches of sex differentiation in CPB: Disruption of <em>dsx</em> leads to feminization of male traits and abnormal female development. Additionally, <em>tra2</em> appears to regulate the alternative splicing of <em>dsx</em>, promoting the production of the female-specific transcripts. This study highlights the pivotal roles of <em>dsx</em> and <em>tra2</em> in CPB sex determination and provides valuable insights into the evolution and diversity of sex determination mechanisms in insects.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"186 ","pages":"Article 104451"},"PeriodicalIF":3.7,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145577126","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The role of the Niemann–Pick type C2 protein as a sperm-binding protein in honeybees","authors":"Jin Myung Kim ,&nbsp;Bo Yeon Kim ,&nbsp;Yun Hui Kim ,&nbsp;Hyung Joo Yoon ,&nbsp;Yong Soo Choi ,&nbsp;Kyeong Yong Lee ,&nbsp;Dong Won Kim ,&nbsp;Kwang Sik Lee ,&nbsp;Byung Rae Jin","doi":"10.1016/j.ibmb.2025.104443","DOIUrl":"10.1016/j.ibmb.2025.104443","url":null,"abstract":"<div><div>The Niemann–Pick type C2 protein (NPC2) functions as a cholesterol modulator in the sperm membrane and enhances sperm physiological functions in vertebrates and some invertebrates. In insects, NPC2 is involved in lipid metabolism, immune response signaling, and chemical communication. However, the role of NPC2 as a sperm-associated protein in insect sperm remains to be elucidated. This study identified a novel function of the <em>Apis mellifera</em> NPC2 protein (AmNPC2) as a sperm-binding protein. Immunoassays and binding assays using recombinant AmNPC2 protein and its specific antibody revealed that AmNPC2 is expressed in the testes of drones and is localized on the sperm surface as a sperm-binding protein. Furthermore, a reduction in AmNPC2 levels on the sperm surface decreased sperm viability. AmNPC2 also appeared to play a protective role in maintaining sperm viability under both oxidative and temperature stress conditions. Our findings indicate that AmNPC2 is a sperm-binding protein that enhances the viability of honeybee sperm.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"186 ","pages":"Article 104443"},"PeriodicalIF":3.7,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145480450","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biotin deficiency bridges metabolic signaling to insecticide sequestration in Nilaparvata lugens","authors":"Mengqing Deng,&nbsp;Xiyue Xu,&nbsp;Zhiming Yang,&nbsp;Kai Lu","doi":"10.1016/j.ibmb.2025.104445","DOIUrl":"10.1016/j.ibmb.2025.104445","url":null,"abstract":"<div><div>Insecticide resistance poses a critical challenge to global agricultural sustainability. While metabolic detoxification and target-site mutations are well-characterized resistance mechanisms, the role of micronutrient homeostasis remains understudied. This study reveals that biotin deficiency in <em>Nilaparvata lugens</em> drives imidacloprid resistance through a multi-tiered regulatory network coordinating chemosensory protein (CSP) dynamics. Biotin deficiency enhances CSP-mediated insecticide sequestration via high-affinity binding to CSP2, CSP4, CSP7, and CSP15, which are overexpressed in resistant strains. RNA interference and dual-luciferase assays demonstrate that the aryl hydrocarbon receptor and its nuclear translocator (AhR/ARNT) transcriptionally activate <em>CSP2</em> and <em>CSP15</em>, with their knockdown partially restoring insecticide susceptibility. Furthermore, biotin deficiency activates reactive oxygen species (ROS)/cap ‘n’ collar C (CncC) signaling, elevating <em>AhR/ARNT</em> expression through transcriptional reprogramming. Yeast three-hybrid assays identify a post-translational regulatory layer, wherein biotin directly inhibits AhR–ARNT heterodimerization. Field-evolved resistant populations recapitulate this mechanism, exhibiting conserved molecular signatures including biotin deficiency, ROS/CncC pathway activation, and AhR/ARNT-CSP overexpression correlated with resistance intensity. These findings establish a unified model wherein biotin scarcity reprograms xenobiotic defense through three synergistic mechanisms: enhanced CSP–insecticide binding, transcriptional amplification via ROS/CncC-AhR/ARNT signaling, and post-translational optimization of transcriptional complexes. The operational conservation of this pathway across laboratory and ecological contexts underscores its evolutionary significance while revealing novel targets for resistance management, particularly biotin-based synergists and AhR dimerization inhibitors.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"186 ","pages":"Article 104445"},"PeriodicalIF":3.7,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145487357","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bombyx mori nucleopolyhedrosis virus-derived circular RNAs with protein-coding potential facilitate viral replication","authors":"Xing Zhang ,&nbsp;Zeen Shen ,&nbsp;Yani Kang ,&nbsp;Wenbin Yu ,&nbsp;Xiaoyan Du ,&nbsp;Qian Teng ,&nbsp;Zihan He ,&nbsp;Chengliang Gong ,&nbsp;Xiaolong Hu","doi":"10.1016/j.ibmb.2025.104420","DOIUrl":"10.1016/j.ibmb.2025.104420","url":null,"abstract":"<div><div>Circular RNAs (circRNAs) are renowned for their exceptional stability and have been increasingly recognized for their dual roles in pro- and antiviral responses during host-virus interactions. In this study, we investigated the functional landscape of circular RNAs (circRNAs) during infection with <em>Bombyx mori</em> nucleopolyhedrosis virus (BmNPV), a model baculovirus system. Our comprehensive analysis revealed that hundreds of host-derived circRNAs are dynamically regulated upon BmNPV infection, while the virus itself generates numerous viral circRNAs (vcircRNAs) via back-splicing. Using a combination of advanced experimental approaches, we validated the existence of multiple cellular and viral circRNAs. Among these, we characterized vcircRNA-390, a BmNPV-encoded circRNA harboring a small open reading frame (ORF) and four viral internal ribosome entry sites (IRESs). Remarkably, vcircRNA-390 serves as a template for the translation of an 81-amino acid viral peptide (VSP81). Functional studies demonstrated that both vcircRNA-390 and VSP81 significantly enhance viral replication. Mechanistically, we provide evidence that VSP81 likely targets the host RNA interference (RNAi) pathway, a major antiviral defence system, to promote viral immune evasion. While these findings establish vcircRNA-390 as a novel proviral factor in insect-virus interactions, the detailed molecular mechanisms by which VSP81 modulates the RNAi machinery remain to be fully elucidated. Our work not only expands the understanding of viral circRNA biology but also reveals a new dimension of the host-pathogen conflict, wherein BmNPV exploits circRNA-mediated translation to subvert antiviral defences.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"185 ","pages":"Article 104420"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145273296","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"V-ATPase B mediates Bt Cry1Ac binding and toxicity in Grapholita molesta","authors":"Dandan Pan ,&nbsp;Jiayang Feng ,&nbsp;Jiacheng Ye,&nbsp;Xiaoyan Yang,&nbsp;Xiaoyan Zhang,&nbsp;Xiaofang Sha,&nbsp;Donghan Wang,&nbsp;Yanshen Fu,&nbsp;Chunxiao Men,&nbsp;Xiangqun Yuan,&nbsp;Yiping Li","doi":"10.1016/j.ibmb.2025.104407","DOIUrl":"10.1016/j.ibmb.2025.104407","url":null,"abstract":"<div><div><em>Grapholita molesta</em> is a worldwide pest. Cry1Ac is a significant alternative <em>Bacillus thuringiensis</em> (Bt) protein that exhibits substantial toxicity towards Lepidoptera insects. This investigation employed ligand blot, SDS-PAGE and liquid chromatography-tandem mass spectrometry (LC-MS/MS) techniques to identify the proteins potentially binding Cry1Ac on the peritrophic membrane (PM) of <em>G. molesta</em>. Real-time quantitative polymerase chain reaction (RT-qPCR) analysis revealed the highest expression of <em>GmolV-ATPase B</em> in the midgut of 4th instar larvae. Following the ingestion of Cry1Ac protoxin by <em>G. molesta</em> larvae, a notable reduction in the expression level of <em>GmolV-ATPase B</em> was observed. The interaction between GmolV-ATPase B and activated Cry1Ac toxin was confirmed through ligand blot and homologous and heterologous competition experiments. Overexpression of GmolV-ATPase B in Sf9 cells led to an increase in Cry1Ac cytotoxicity, while RNAi targeting <em>GmolV-ATPase B</em> resulted in reduced mortality. In vivo bioassays demonstrated that the combined action of GmolV-ATPase B protein and Cry1Ac protoxin significantly enhanced the toxicity of Cry1Ac towards <em>G. molesta</em> larvae compared to Cry1Ac alone. These findings shed light on the binding of Cry1Ac to PM of <em>G. molesta</em> and its insecticidal mechanism, offering a valuable important reference for the development of biopesticides targeting midgut PM proteins.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"185 ","pages":"Article 104407"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145172182","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Assessment of RNA interference effectiveness mediated by siRNA sequences and structures in Drosophila S2 cells","authors":"Hyun-Soo Kim ,&nbsp;Huipeng Pan ,&nbsp;Subba Reddy Palli ,&nbsp;June-Sun Yoon","doi":"10.1016/j.ibmb.2025.104418","DOIUrl":"10.1016/j.ibmb.2025.104418","url":null,"abstract":"<div><div>Extensive research has clarified the mechanisms of RNA interference (RNAi) in insects. Although double-stranded RNA (dsRNA) effectively induces RNAi in insects, comprehensive studies on how small interfering RNA (siRNA) structural characteristics influence messenger RNA (mRNA) cleavage efficiency are limited. This study systematically examined the impact of diverse sequence and structural modifications on the efficiency of siRNA-mediated knockdown of target genes in <em>Drosophila melanogaster</em>. Our findings indicate that siRNA efficacy drastically decreased at a length of 17 nucleotides (nt), but was restored by extending to 19 base pairs (bp) with random sequences. Additionally, siRNAs with 2-nt overhangs demonstrated greater efficacy compared to blunt-ended structures. We found that the knockdown efficiency varies depending on the secondary structure characteristics of the mRNA region to which siRNA binds. Furthermore, next-generation sequencing was employed to map predicted siRNA distributions to actual dsRNA processing patterns, allowing detailed profiling of cleavage depth and sequence preferences. Collectively, these results enhance our understanding of the relationship between siRNA sequence design parameters and RNAi efficiency in <em>Drosophila</em>, providing a significant advance in siRNA-based RNAi research in insects. This study also offers valuable insights into dsRNA off-target effects.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"185 ","pages":"Article 104418"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145256973","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"HSF-1 regulates FoxO expression to induce diapause in the cotton bollworm, Helicoverpa armigera via upstream HIF-1α and MNK signaling","authors":"Zhi-Ren Su,&nbsp;Xiao-Long Su,&nbsp;Song-Shan Jiang,&nbsp;Wei-Hua Xu","doi":"10.1016/j.ibmb.2025.104429","DOIUrl":"10.1016/j.ibmb.2025.104429","url":null,"abstract":"<div><div>Diapause is a widespread adaptation of insects that allows for them to survive under environmental stress by activating different gene clusters to inhibit metabolism and delay development. Previous studies have shown that reactive oxygen species (ROS) in brains of diapause-destined pupae of the cotton bollworm <em>Helicoverpa armigera</em> activate hypoxia-inducible factor-1α (HIF-1α), a transcription factor, to induce diapause. However, the molecular mechanism by which HIF-1α induces diapause remains unclear. In this study, a high abundance of heat shock factor-1 (HSF-1) protein, a transcription factor, was detected in brains of diapause-destined pupae, and phosphorylated HSF-1 was its active form. HSF-1 was phosphorylated by the protein kinase MNK, a member of the mitogen-activated protein kinase (MAPK) family. Moreover, the transcription of <em>MNK</em> was regulated by HIF-1α. Activated HSF-1 then promoted the expression of <em>FoxO</em>, which is the master regulator that triggers slow development to induce diapause. These results suggest that the HIF-1α/MNK/HSF-1/FoxO regulatory pathway promotes insect diapause.</div></div>","PeriodicalId":330,"journal":{"name":"Insect Biochemistry and Molecular Biology","volume":"185 ","pages":"Article 104429"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145399245","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}