Pub Date : 2026-08-01Epub Date: 2026-08-06DOI: 10.1016/j.tibs.2026.06.007
Miguel A. De la Rosa
Since 1964, the Federation of European Biochemical Societies has supported the molecular life sciences through scientific exchange, training, international collaboration, and publishing. This study provides an overview of the organisation’s evolution, activities, initiatives, and its contributions to supporting researchers and scientific communities across Europe and beyond.
{"title":"Building scientific communities for the future of the molecular life sciences: The role of FEBS","authors":"Miguel A. De la Rosa","doi":"10.1016/j.tibs.2026.06.007","DOIUrl":"10.1016/j.tibs.2026.06.007","url":null,"abstract":"<div><div>Since 1964, the Federation of European Biochemical Societies has supported the molecular life sciences through scientific exchange, training, international collaboration, and publishing. This study provides an overview of the organisation’s evolution, activities, initiatives, and its contributions to supporting researchers and scientific communities across Europe and beyond.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 8","pages":"Pages 749-751"},"PeriodicalIF":14.4,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148683072","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-08-01Epub Date: 2026-05-01DOI: 10.1016/j.tibs.2026.04.006
Hsin-Yen Larry Wu, Polly Yingshan Hsu
The formation of xylem vessels depends on a balance between transcription factors SACLs and LHW, whose translation is controlled by thermospermine. A recent study shows that a conserved rRNA methylation by OVERACHIEVER enables thermospermine binding, allowing ribosomes to oppositely regulate SACL and LHW translation to direct plant xylem cell fate.
{"title":"Thermospermine drives dual-action ribosomes to shape plant xylem development","authors":"Hsin-Yen Larry Wu, Polly Yingshan Hsu","doi":"10.1016/j.tibs.2026.04.006","DOIUrl":"10.1016/j.tibs.2026.04.006","url":null,"abstract":"<div><div>The formation of xylem vessels depends on a balance between transcription factors SACLs and LHW, whose translation is controlled by thermospermine. <span><span>A recent study</span><svg><path></path></svg></span> shows that a conserved rRNA methylation by OVERACHIEVER enables thermospermine binding, allowing ribosomes to oppositely regulate <em>SACL</em> and <em>LHW</em> translation to direct plant xylem cell fate.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 8","pages":"Pages 752-754"},"PeriodicalIF":14.4,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147809057","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}
Pub Date : 2026-08-01Epub Date: 2026-05-20DOI: 10.1016/j.tibs.2026.04.012
José E. Pérez-Ortín, Sebastián Chávez, Mordechai Choder
RNA imprinting refers to the co-transcriptional binding of (a) factor(s) that remain associated with the RNA as it enters the cytoplasm, where it/they regulate(s) post-transcriptional processes. Transcription factors (TFs), such as yeast Sfp1 and mammalian tristetraprolin, FUS, and Yin–Yang 1, exemplify RNA imprinting by zinc-binding proteins. These TFs contain large intrinsically disordered regions (IDRs) and have the capacity to bind both DNA and RNA. The most prevalent zinc-binding domains among TFs are zinc fingers (ZFs), which recognize nucleic acids through modular tandem arrangements. We hypothesize that the structural organization of ZFs enables switching between DNA and RNA during transcription. The IDRs of these TFs, together with the nascent RNA, contribute to transcription-related biomolecular condensates that may facilitate this switching, enabling their imprinting.
{"title":"RNA imprinting by zinc-finger proteins","authors":"José E. Pérez-Ortín, Sebastián Chávez, Mordechai Choder","doi":"10.1016/j.tibs.2026.04.012","DOIUrl":"10.1016/j.tibs.2026.04.012","url":null,"abstract":"<div><div>RNA imprinting refers to the co-transcriptional binding of (a) factor(s) that remain associated with the RNA as it enters the cytoplasm, where it/they regulate(s) post-transcriptional processes. Transcription factors (TFs), such as yeast Sfp1 and mammalian tristetraprolin, FUS, and Yin–Yang 1, exemplify RNA imprinting by zinc-binding proteins. These TFs contain large intrinsically disordered regions (IDRs) and have the capacity to bind both DNA and RNA. The most prevalent zinc-binding domains among TFs are zinc fingers (ZFs), which recognize nucleic acids through modular tandem arrangements. We hypothesize that the structural organization of ZFs enables switching between DNA and RNA during transcription. The IDRs of these TFs, together with the nascent RNA, contribute to transcription-related biomolecular condensates that may facilitate this switching, enabling their imprinting.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 8","pages":"Pages 761-773"},"PeriodicalIF":14.4,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147979907","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}
Pub Date : 2026-08-01Epub Date: 2026-06-24DOI: 10.1016/j.tibs.2026.05.013
Madouc D. Bergers, Tessa A. Goté, Zachary Armstrong
Glycans are polymeric carbohydrate chains that often decorate proteins and lipids present on cell surfaces and in the extracellular space, thereby influencing cell interactions, immune responses, and host–microbiome relationships. Glycans are highly dynamic and can undergo a plethora of post-synthetic modifications, including O-acetylation, sulfation, and sulfamation. In this review, we examine how these glycan modifications are established and how they influence human health, from cell signaling to host–pathogen dynamics. We propose terming these glycan modifications, which give rise to a greater diversity of glycans, collectively as the epiglycome. Despite their biological importance, glycan modifications are considerably less well studied than the underlying glycans and proteins. However, advances in chemical and biochemical tools are enabling greater insights into their roles and translational potential.
{"title":"The role of glycan modifications in health and disease","authors":"Madouc D. Bergers, Tessa A. Goté, Zachary Armstrong","doi":"10.1016/j.tibs.2026.05.013","DOIUrl":"10.1016/j.tibs.2026.05.013","url":null,"abstract":"<div><div>Glycans are polymeric carbohydrate chains that often decorate proteins and lipids present on cell surfaces and in the extracellular space, thereby influencing cell interactions, immune responses, and host–microbiome relationships. Glycans are highly dynamic and can undergo a plethora of post-synthetic modifications, including <em>O</em>-acetylation, sulfation, and sulfamation. In this review, we examine how these glycan modifications are established and how they influence human health, from cell signaling to host–pathogen dynamics. We propose terming these glycan modifications, which give rise to a greater diversity of glycans, collectively as the epiglycome. Despite their biological importance, glycan modifications are considerably less well studied than the underlying glycans and proteins. However, advances in chemical and biochemical tools are enabling greater insights into their roles and translational potential.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 8","pages":"Pages 787-800"},"PeriodicalIF":14.4,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148315143","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}
Pub Date : 2026-08-01Epub Date: 2026-07-06DOI: 10.1016/j.tibs.2026.05.012
Ghazanfar Abbas Khan, Elycia Calvet, Jean-Luc Battini, Yves Poirier
Inorganic phosphate (Pi) is an essential macronutrient, and tight regulation of Pi import and export is required to maintain Pi homeostasis. Although Pi import mechanisms have been extensively characterized, the molecular basis of Pi export has only recently begun to emerge. Arabidopsis PHOSPHATE 1 (PHO1) and its homologue PHO1;H1 are prototypical members of the SPX [Syg1/PHO81/xenotropic and polytropic retrovirus receptor 1 (XPR1)]–EXS (ERD1/XPR1/SYG1) family of Pi exporters conserved throughout eukaryotes, including the metazoan orthologue XPR1 and fungal SYG1. We review recent structural studies redefining XPR1 and PHO1;H1 Pi transporters as channel-like proteins using a double-lock gating mechanism controlled by inositol pyrophosphates. This new knowledge enhances our ability to modulate the activity of SPX–EXS proteins involved in human diseases, such as cancer, as well as enhance phosphate-use efficiency in crops.
{"title":"A unified mechanism of phosphate export across eukaryotes through EXS domain-containing proteins","authors":"Ghazanfar Abbas Khan, Elycia Calvet, Jean-Luc Battini, Yves Poirier","doi":"10.1016/j.tibs.2026.05.012","DOIUrl":"10.1016/j.tibs.2026.05.012","url":null,"abstract":"<div><div>Inorganic phosphate (Pi) is an essential macronutrient, and tight regulation of Pi import and export is required to maintain Pi homeostasis. Although Pi import mechanisms have been extensively characterized, the molecular basis of Pi export has only recently begun to emerge. <em>Arabidopsis</em> PHOSPHATE 1 (PHO1) and its homologue PHO1;H1 are prototypical members of the SPX [Syg1/PHO81/xenotropic and polytropic retrovirus receptor 1 (XPR1)]–EXS (ERD1/XPR1/SYG1) family of Pi exporters conserved throughout eukaryotes, including the metazoan orthologue XPR1 and fungal SYG1. We review recent structural studies redefining XPR1 and PHO1;H1 Pi transporters as channel-like proteins using a double-lock gating mechanism controlled by inositol pyrophosphates. This new knowledge enhances our ability to modulate the activity of SPX–EXS proteins involved in human diseases, such as cancer, as well as enhance phosphate-use efficiency in crops.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 8","pages":"Pages 774-786"},"PeriodicalIF":14.4,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148395215","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-08-01Epub Date: 2026-06-18DOI: 10.1016/j.tibs.2026.05.008
Chengrui Hu (胡乘睿), Yourong Pan (潘有容), Chengxi Li (李承喜)
{"title":"CycloPepper learns cyclization sites in therapeutic peptides","authors":"Chengrui Hu (胡乘睿), Yourong Pan (潘有容), Chengxi Li (李承喜)","doi":"10.1016/j.tibs.2026.05.008","DOIUrl":"10.1016/j.tibs.2026.05.008","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 8","pages":"Pages 844-845"},"PeriodicalIF":14.4,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148275412","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}
Pub Date : 2026-08-01Epub Date: 2026-08-06DOI: 10.1016/j.tibs.2026.06.006
Tamor A. Khan
{"title":"Musings of a lab janitor: Data analysis","authors":"Tamor A. Khan","doi":"10.1016/j.tibs.2026.06.006","DOIUrl":"10.1016/j.tibs.2026.06.006","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 8","pages":"Page 846"},"PeriodicalIF":14.4,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148683122","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-08-01Epub Date: 2026-03-31DOI: 10.1016/j.tibs.2026.02.017
Nicolas Rivard, Julius Martinkus, Margot M. Dessartine, Jean-Philippe Côté, Eric Cascales
Survival of bacteria in dense and competitive microbial communities depends on their ability to access nutrients or outcompete neighboring cells. One of the key players in competition is the type VI secretion system (T6SS), a contractile nanomachine that injects a broad variety of effectors into competitors. However, target cells do not remain defenseless. Given the lethality of T6SS-mediated attacks, they have evolved countermeasures to detect, withstand, or resist such assaults: immunity proteins that neutralize effectors, activation of envelope stress pathways to mitigate damage, retaliatory responses to avoid recurrent attacks, physical barriers such as matrix polymers, or collective protection through aggregation. In this review article, we provide a comprehensive overview of these diverse strategies and emphasize the arms-race dynamics.
{"title":"Anti-type VI tactics: bacterial defenses against type VI secretion system attacks","authors":"Nicolas Rivard, Julius Martinkus, Margot M. Dessartine, Jean-Philippe Côté, Eric Cascales","doi":"10.1016/j.tibs.2026.02.017","DOIUrl":"10.1016/j.tibs.2026.02.017","url":null,"abstract":"<div><div>Survival of bacteria in dense and competitive microbial communities depends on their ability to access nutrients or outcompete neighboring cells. One of the key players in competition is the type VI secretion system (T6SS), a contractile nanomachine that injects a broad variety of effectors into competitors. However, target cells do not remain defenseless. Given the lethality of T6SS-mediated attacks, they have evolved countermeasures to detect, withstand, or resist such assaults: immunity proteins that neutralize effectors, activation of envelope stress pathways to mitigate damage, retaliatory responses to avoid recurrent attacks, physical barriers such as matrix polymers, or collective protection through aggregation. In this review article, we provide a comprehensive overview of these diverse strategies and emphasize the arms-race dynamics.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 8","pages":"Pages 816-826"},"PeriodicalIF":14.4,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147589096","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-08-01Epub Date: 2026-08-06DOI: 10.1016/S0968-0004(26)00228-8
{"title":"Subscription and Copyright Information","authors":"","doi":"10.1016/S0968-0004(26)00228-8","DOIUrl":"10.1016/S0968-0004(26)00228-8","url":null,"abstract":"","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 8","pages":"Page e1"},"PeriodicalIF":14.4,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148745748","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}
Pub Date : 2026-08-01Epub Date: 2026-06-17DOI: 10.1016/j.tibs.2026.05.010
Nicholas W. Hubbard, Nels C. Elde
Fels et al. (2026) report that the giant DNA virus mimivirus encodes a complete, functional translation initiation complex, termed vIF4F, which replaces the host’s own initiation machinery during infection, sustains viral protein synthesis under cellular stress, and points to a blurring of boundaries between viral and cellular life.
{"title":"Cap in hand: giant viruses, stolen translation, and a road to endosymbiosis?","authors":"Nicholas W. Hubbard, Nels C. Elde","doi":"10.1016/j.tibs.2026.05.010","DOIUrl":"10.1016/j.tibs.2026.05.010","url":null,"abstract":"<div><div><span><span>Fels <em>et al</em>.</span><svg><path></path></svg></span> (2026) report that the giant DNA virus mimivirus encodes a complete, functional translation initiation complex, termed vIF4F, which replaces the host’s own initiation machinery during infection, sustains viral protein synthesis under cellular stress, and points to a blurring of boundaries between viral and cellular life.</div></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"51 8","pages":"Pages 755-757"},"PeriodicalIF":14.4,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148269820","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}
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