Zi-Liang Hu , Hong Wei , Linfeng Sun , Eugenia Russinova
{"title":"Plant steroids on the move: mechanisms of brassinosteroid export","authors":"Zi-Liang Hu , Hong Wei , Linfeng Sun , Eugenia Russinova","doi":"10.1016/j.tibs.2025.03.003","DOIUrl":"10.1016/j.tibs.2025.03.003","url":null,"abstract":"<div><div>Brassinosteroids (BRs) are essential plant steroidal hormones that regulate growth and development. The recent discoveries of ATP-binding cassette subfamily B (ABCB) members, ABCB19 and ABCB1, as BR transporters highlight the significance of active export to the apoplast in maintaining BR homeostasis and enabling effective signaling. This review focuses on the latest progress in understanding ABCB-mediated BR transport, with particular attention to the structural and functional characterization of arabidopsis ABCB19 and ABCB1. These findings reveal both conserved and distinct features in substrate recognition and transport mechanisms, providing valuable insights into their roles in hormonal regulation. Additionally, the evolutionary conservation of ABC transporters in mediating steroid-based signaling across biological kingdoms underscores their fundamental biological significance.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 6","pages":"Pages 508-519"},"PeriodicalIF":11.6,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143956848","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ayoola B. Smith , Renee C. Ejindu , Jonathan R. Chekan
{"title":"Engineering RiPP pathways: strategies for generating complex bioactive peptides","authors":"Ayoola B. Smith , Renee C. Ejindu , Jonathan R. Chekan","doi":"10.1016/j.tibs.2025.04.001","DOIUrl":"10.1016/j.tibs.2025.04.001","url":null,"abstract":"<div><div>Historically, natural products have been essential sources of therapeutic agents, many of which are currently used to manage various diseases. In recent years, ribosomally synthesized and post-translationally modified peptides (RiPPs) have garnered considerable interest in drug discovery and development due to their biosynthetic plasticity and their ability to generate diverse bioactive structural scaffolds. Unfortunately, many RiPPs have suboptimal bioavailability and proteolytic stability, significantly limiting their clinical potential. Moreover, the complexity of RiPP structures makes total synthesis extremely difficult. These drawbacks necessitate pathway engineering to create derivatives with potentially optimized physicochemical properties. Herein, we review recent efforts to surmount pathway engineering challenges and to rationally modify components of RiPP pathways for new functions to derive new bioactive analogs.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 6","pages":"Pages 495-507"},"PeriodicalIF":11.6,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143960087","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Advisory Board and Contents","authors":"","doi":"10.1016/S0968-0004(25)00113-6","DOIUrl":"10.1016/S0968-0004(25)00113-6","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 6","pages":"Pages i-ii"},"PeriodicalIF":11.6,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144212723","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Modifying the modifiers: ubiquitination of ADP-ribosylation in human cells","authors":"Karla L.H. Feijs-Žaja , Jonas Siefert , Roko Žaja","doi":"10.1016/j.tibs.2025.03.010","DOIUrl":"10.1016/j.tibs.2025.03.010","url":null,"abstract":"<div><div>Ubiquitination and ADP-ribosylation are protein post-translational modifications (PTMs) which influence diverse protein properties. <em>In vitro</em> work has indicated that ubiquitin can be ADP-ribosylated and vice versa, ADP-ribose ubiquitinated. An exciting new study by <span><span>Bejan <em>et al</em></span><svg><path></path></svg></span>. now demonstrates that ubiquitination of ADP-ribosylated proteins, termed MARUbylation, occurs in human cells.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 6","pages":"Pages 461-463"},"PeriodicalIF":11.6,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143951822","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Thermal proteome profiling of protein-centric interactions and modifications","authors":"Zhenghui Chen , Anhui Wang , Yiqun Geng","doi":"10.1016/j.tibs.2025.02.002","DOIUrl":"10.1016/j.tibs.2025.02.002","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 6","pages":"Pages 544-545"},"PeriodicalIF":11.6,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143655572","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Laetitia Coassolo , Katrin J. Svensson , Caitlin L. Gare , Andrew M. White , Lara R. Malins , Ayoola B. Smith , Jonathan R. Chekan
{"title":"Harnessing the power of peptides: advances and collaborations in biochemistry","authors":"Laetitia Coassolo , Katrin J. Svensson , Caitlin L. Gare , Andrew M. White , Lara R. Malins , Ayoola B. Smith , Jonathan R. Chekan","doi":"10.1016/j.tibs.2025.05.001","DOIUrl":"10.1016/j.tibs.2025.05.001","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 6","pages":"Pages 458-460"},"PeriodicalIF":11.6,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144131963","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Laetitia Coassolo , Amanda Wiggenhorn , Katrin J. Svensson
{"title":"Understanding peptide hormones: from precursor proteins to bioactive molecules","authors":"Laetitia Coassolo , Amanda Wiggenhorn , Katrin J. Svensson","doi":"10.1016/j.tibs.2025.03.014","DOIUrl":"10.1016/j.tibs.2025.03.014","url":null,"abstract":"<div><div>Peptide hormones are fundamental regulators of biological processes involved in homeostasis regulation and are often dysregulated in endocrine diseases. Despite their biological significance and established therapeutic potential, there is still a gap in our knowledge of their processing and post-translational modifications, as well as in the technologies for their discovery and detection. In this review, we cover insights into the peptidome landscape, including the proteolytic processing and post-translational modifications of peptide hormones. Understanding the full landscape of peptide hormones and their modifications could provide insights into leveraging proteolytic mechanisms to identify novel peptides with therapeutic potential. Therefore, we also discuss the need for future research aiming at better predicting, detecting, and characterizing new peptides with biological activities.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"50 6","pages":"Pages 481-494"},"PeriodicalIF":11.6,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143956608","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"From disorder to order: cryo-EM reveals RNA-dependent remodeling of Nipah virus polymerase.","authors":"Rupesh Balaji Jayachandran, Max Renner","doi":"10.1016/j.tibs.2025.05.003","DOIUrl":"https://doi.org/10.1016/j.tibs.2025.05.003","url":null,"abstract":"<p><p>A flurry of recent structural studies have focused on the polymerase complex of the deadly zoonotic pathogen Nipah virus (NiV). These include a report by Sala et al. describing an RNA duplex-bound state. This structure constitutes a snapshot of the complex in an early elongation step of the RNA synthesis cycle.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":11.6,"publicationDate":"2025-05-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144223917","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Juliane Tschuck, Vera Skafar, José Pedro Friedmann Angeli, Kamyar Hadian
{"title":"The metabolic code of ferroptosis: nutritional regulators of cell death.","authors":"Juliane Tschuck, Vera Skafar, José Pedro Friedmann Angeli, Kamyar Hadian","doi":"10.1016/j.tibs.2025.04.007","DOIUrl":"https://doi.org/10.1016/j.tibs.2025.04.007","url":null,"abstract":"<p><p>Ferroptosis is a distinctive form of regulated cell death driven by iron-dependent phospholipid peroxidation. Its initiation and suppression are finely tuned by metabolic pathways, transcription factors, and nuclear receptors that control lipid peroxidation levels. Significantly, nutrients such as vitamins and trace elements play a pivotal role in this regulation, directly linking diet and nutrients to cellular fate. This review conveys the latest insights into the metabolic components that influence ferroptosis. We highlight how metabolic and transcriptional regulators and key nutrients, micronutrients, and metabolites orchestrate this process. Charting these interactions will be essential for developing new avenues for therapeutic interventions targeting ferroptosis in various diseases.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":11.6,"publicationDate":"2025-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144179485","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Marion Jespersen, Chris Greening, Leonard Ernst, Pok Man Leung, Hannah S Shafaat, Rhys Grinter
{"title":"Diverse lineages and adaptations of oxygen-adapted hydrogenases.","authors":"Marion Jespersen, Chris Greening, Leonard Ernst, Pok Man Leung, Hannah S Shafaat, Rhys Grinter","doi":"10.1016/j.tibs.2025.04.006","DOIUrl":"https://doi.org/10.1016/j.tibs.2025.04.006","url":null,"abstract":"<p><p>Hydrogenases allow microorganisms to consume and produce hydrogen gas (H<sub>2</sub>). Although most hydrogenases are oxygen (O<sub>2</sub>)-sensitive, recent studies show that bacteria and archaea produce diverse nickel-iron [NiFe]-hydrogenases that function in oxic environments and often support aerobic respiration. As we describe herein, these hydrogenases have independently evolved multiple strategies to withstand O<sub>2</sub>, not only by reversing inhibition through reduction of bound O<sub>2</sub> to water using a unique [4Fe3S] cluster but also by preventing O<sub>2</sub> binding through narrow gas channels and active-site rearrangements. We further propose that [NiFe]-hydrogenases originated on an anoxic Earth, but diversified after the Great Oxygenation Event to tolerate and exploit redox coupling with O<sub>2</sub>. Hydrogenases may be more adaptable to O<sub>2</sub> than was previously thought, and this has implications for synthetic biology and biomimetics.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":11.6,"publicationDate":"2025-05-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144172024","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}