Serving the scientific community: FEBS Open Bio in 2024.

FEBS Open Bio is committed to not only publishing sound science but also to supporting early-career researchers and the scientific community as a whole. In this editorial, we look back at how the journal recognised and rewarded excellent research in 2023 and look forward to 2024.

FEBS fellowships: supporting excellent science for over four decades.

The Federation of European Biochemical Societies (FEBS) awarded FEBS Long-Term Fellowships from 1979 until 2020, at which time the scheme was replaced with the FEBS Excellence Award. Over four decades, FEBS awarded a huge number of Long-Term Fellowships, helping to support and promote the careers of excellent young researchers across Europe. To celebrate the exciting work performed by the FEBS Long-Term Fellows, we present here a special 'In the Limelight' issue of FEBS Open Bio, containing four Mini-reviews and four Research Protocols authored by the fellows themselves. The four Review articles provide timely updates on the respective research fields, while the Research Protocols describe how to perform challenging experimental methods in detail. We hope this issue will be a valuable resource for the community, and a celebration of the high-quality work done by young scientists.

Innovation and renovation: FEBS Open Bio in 2023.

FEBS Open Bio is constantly evolving to best suit the needs of the scientific community. In this Editorial, we review the various new initiatives introduced in 2022 and look forward to the opportunities and challenges that lie ahead in 2023.

Ensuring image integrity in the digital age.

FEBS Open Bio and our fellow FEBS Press journals have a strong commitment to maintaining the integrity of the scientific literature. The life sciences, in particular, are suffering from an ongoing reproducibility crisis, and this may in part be fuelled by mistakes, manipulation or outright fabrication of the presented data. We were recently made aware of several articles published in FEBS Open Bio that appear to contain full or partial duplications of images from other published articles in a different scientific context. In most of these cases, the duplications were taken from previously published papers. After thorough investigation and subsequent discussion within FEBS Press and with Wiley's Integrity in Publishing Group, we have retracted most of these articles.

An open chat with Laszlo Nagy.

Laszlo Nagy has been on the Editorial Board of FEBS Open Bio since the journal's inception and is a passionate supporter of FEBS Press and other society journals. Currently, he is also an editor of FEBS Letters and The Journal of Clinical Investigation (JCI). He studied medicine at the University Medical School of Debrecen in Hungary, where he graduated with an M.D. and later Ph.D., and then moved to the United States to conduct postdoctoral research at the University of Texas-Houston and subsequently the Salk Institute in San Diego. Laszlo is a Professor of Medicine and Biological Chemistry at John Hopkins School of Medicine, where he is Co-Director of the Institute for Fundamental Biomedical Research and Associate Director of the Center for Metabolic Origins of Disease, and Adjunct Professor at the University of Debrecen. Formerly, he was a Professor and Founding Director of the Genomic Control of Metabolism Program at the Sanford Burnham Prebys Medical Discovery Institute. He is also a member of the European Molecular Biology Organisation (EMBO), Academia Europaea, the Hungarian Academy of Sciences and The Henry Kunkel Society, and recipient of several awards, including the Boehringer Ingelheim Research Award, Cheryl Whitlock/Pathology Prize, a Wellcome Trust Senior Research Fellowship in Biomedical Sciences, and three Howard Hughes Medical Institute International Research Scholar Awards. In this fascinating interview, Laszlo Nagy shares the advice that changed his career trajectory, relates his views on scientific publishing, discusses new developments at The Johns Hopkins Center for Metabolic Origins of Disease, and outlines the prospects for future development of research and technology infrastructures in eastern Europe.

Entering the second decade: FEBS Open Bio in 2022.

FEBS Open Bio continues to go from strength to strength, with 2021 perhaps marking its most exciting year. In this Editorial, the Editor-in-Chief Miguel A. De la Rosa looks back at all the new developments of 2021 and forecasts the outlook for 2022.

FEBS Open Bio: past, present and future.

In celebration of the 10th anniversary of FEBS Open Bio, we spoke to some of the key figures of the journal's genesis, development, and its future direction, and recount here their thoughts and experiences. Prof. Félix. Goñi discusses the role of the FEBS Publication Committee in the journal's beginnings, Dr Mary Purton relates her experiences as the journal's Executive Editor, Prof. László Fésüs explains how the journal developed during his tenure as Chair of the Publication Committee, and Prof. Johannes Buchner looks forward to the future of FEBS Press and academic publishing. Finally, Prof. John (Iain) Mowbray describes his "Friday afternoon thought" to start a new journal.

Ten years of FEBS Open Bio.

This month, FEBS Open Bio celebrates its 10th birthday. To celebrate the journal's first decade, we present this special anniversary issue, comprised of editorials, reviews, and research articles especially commissioned for the occasion. In this introductory editorial, we invite the reader to join us as we reminisce over the journal's past, celebrate its present, and look forward to its future.

(Ubi)quitin' the h2bit: recent insights into the roles of H2B ubiquitylation in DNA replication and transcription.

The reversible ubiquitylation of histone H2B has long been known to regulate gene transcription, and is now understood to modulate DNA replication as well. In this review, we describe how recent, genome-wide analyses have demonstrated that this histone mark has further reaching effects on transcription and replication than once thought. We also consider the ongoing efforts to elucidate the molecular mechanisms by which H2B ubiquitylation affects processes on the DNA template, and outline the various hypothetical scenarios.

The C-terminus of histone H2B is involved in chromatin compaction specifically at telomeres, independently of its monoubiquitylation at lysine 123.

Telomeric heterochromatin assembly in budding yeast propagates through the association of Silent Information Regulator (SIR) proteins with nucleosomes, and the nucleosome array has been assumed to fold into a compacted structure. It is believed that the level of compaction and gene repression within heterochromatic regions can be modulated by histone modifications, such as acetylation of H3 lysine 56 and H4 lysine 16, and monoubiquitylation of H2B lysine 123. However, it remains unclear as to whether or not gene silencing is a direct consequence of the compaction of chromatin. Here, by investigating the role of the carboxy-terminus of histone H2B in heterochromatin formation, we identify that the disorderly compaction of chromatin induced by a mutation at H2B T122 specifically hinders telomeric heterochromatin formation. H2B T122 is positioned within the highly conserved AVTKY motif of the αC helix of H2B. Heterochromatin containing the T122E substitution in H2B remains inaccessible to ectopic dam methylase with dramatically increased mobility in sucrose gradients, indicating a compacted chromatin structure. Genetic studies indicate that this unique phenotype is independent of H2B K123 ubiquitylation and Sir4. In addition, using ChIP analysis, we demonstrate that telomere structure in the mutant is further disrupted by a defect in Sir2/Sir3 binding and the resulting invasion of euchromatic histone marks. Thus, we have revealed that the compaction of chromatin per se is not sufficient for heterochromatin formation. Instead, these results suggest that an appropriately arrayed chromatin mediated by H2B C-terminus is required for SIR binding and the subsequent formation of telomeric chromatin in yeast, thereby identifying an intrinsic property of the nucleosome that is required for the establishment of telomeric heterochromatin. This requirement is also likely to exist in higher eukaryotes, as the AVTKY motif of H2B is evolutionarily conserved.

Alternative splicing in the voltage-gated sodium channel DmNav regulates activation, inactivation, and persistent current.

Diversity in neuronal signaling is a product not only of differential gene expression, but also of alternative splicing. However, although recognized, the precise contribution of alternative splicing in ion channel transcripts to channel kinetics remains poorly understood. Invertebrates, with their smaller genomes, offer attractive models to examine the contribution of splicing to neuronal function. In this study we report the sequencing and biophysical characterization of alternative splice variants of the sole voltage-gated Na+ gene (DmNav, paralytic), in late-stage embryos of Drosophila melanogaster. We identify 27 unique splice variants, based on the presence of 15 alternative exons. Heterologous expression, in Xenopus oocytes, shows that alternative exons j, e, and f primarily influence activation kinetics: when present, exon f confers a hyperpolarizing shift in half-activation voltage (V1/2), whereas j and e result in a depolarizing shift. The presence of exon h is sufficient to produce a depolarizing shift in the V1/2 of steady-state inactivation. The magnitude of the persistent Na+ current, but not the fast-inactivating current, in both oocytes and Drosophila motoneurons in vivo is directly influenced by the presence of either one of a pair of mutually exclusive, membrane-spanning exons, termed k and L. Transcripts containing k have significantly smaller persistent currents compared with those containing L. Finally, we show that transcripts lacking all cytoplasmic alternatively spliced exons still produce functional channels, indicating that splicing may influence channel kinetics not only through change to protein structure, but also by allowing differential modification (i.e., phosphorylation, binding of cofactors, etc.). Our results provide a functional basis for understanding how alternative splicing of a voltage-gated Na+ channel results in diversity in neuronal signaling.