Browse Articles

Structures of complete extracellular receptor assemblies mediated by the pro-inflammatory cytokines IL-12 and IL-23 reveal key commonalities and diverse features, with only IL-12 juxtaposing receptor domains proximal to the cell membrane.

The authors report the structure of a human 48S translation initiation complex, finding a second molecule of eIF4A at the mRNA entry site, apart from the one present within the cap-binding complex eIF4F. This second entry-site eIF4A may be responsible for unwinding mRNA secondary structure.

This study reveals the mechanism by which protons gate a CLC-type Cl⁻/H⁺ exchanger. The authors show that pH-dependent concerted structural rearrangements open the H⁺ pathway, which allosterically enables the Cl⁻ pore opening and ion exchange.

Liu et al. show how cortactin stabilizes Arp2/3 actin branches by binding the daughter filament. It stabilizes the interface of activated Arp3 with the first actin subunit of the new filament, and its central repeats extend along successive daughter-filament subunits.

Structural and biochemical studies show PU.1 facilitates C/EBPa binding to the CX3CR1 nucleosome by interacting with histone H2A and shifting the DNA position, leading to unwrapping of nucleosomal DNA and opening of the H1-condensed nucleosome array.

January 2024 marks 30 years since we published our first volume. Throughout the upcoming year, we will be celebrating this milestone, reflecting on the road covered and looking toward the future — with the help of our readers.

Collaboration is key to modern science, with major advances using multiple complementary approaches and dependent on sophisticated infrastructure. Yet science is also highly personal, as each person carves out a reputation and career. How does this work out in reality, and how can communities be built to benefit science and scientists?

Here we investigate the role of epigenetics in the formation, transcription regulation, maintenance and termination of several non-canonical chromatin structures. Using two examples, we demonstrate how studying non-canonical structures may reveal underlying mechanisms with implications for disease and propose intriguing epigenetic avenues for further exploration.

Here the authors report that TFAP2C and NR5A2, two TF lineage regulators, activate both inner cell mass and trophectoderm programs in totipotent mouse embryos, leading to ‘bipotency activation’ to initiate the first cell-fate specification.

Using a combination of bioinformatics, biochemistry, genetics, genomics and cell-based approaches, this study shows that the H3–H4 binding capacity of the histone chaperone SPT2 is required to preserve chromatin structure and function in Metazoa.

In this study, Asami et al. present the cryo-EM structure of the complex between hepatitis B virus protein and its host entry receptor NTCP, which provide a blueprint for the rational design of anti-HBV drugs targeting virus entry.

Here, the authors discuss the various roles of the HUSH transcriptional silencing complex and its dysregulation in disease.

MRP4 is an ATP-binding cassette transporter that transports prostanoids, a group of signaling molecules. The authors use cryo-EM to visualize the transport cycle and characterize its substrate selectivity.

Here, the authors structurally characterize two sequential complexes leading to prespliceosome assembly, providing insights into the mechanism of branch site proofreading in the human spliceosome.

Using targeted proteomics, the authors reveal concurrent mitotic binding of nuclear receptors, a super-family of transcription factors that emerge as recurrent mitotic bookmarking factors, promoting the reactivation of the pluripotency network in embryonic stem cells.

In intracellular trafficking, transport vesicles deliver cargo via membrane fusion. The fusion machinery includes both tethering factors and SNAREs. The cryo-electron microscopy structure of a tether–SNARE complex reveals the basis for their collaboration.

The concluding statement of Watson and Crick’s historic paper on the structure of DNA¹ enshrines a key tenet of molecular mechanistic cell biology: “… the specific pairing we have postulated immediately suggests a possible copying mechanism for the genetic material”. Function — heredity in this case — is embedded in the redundant sequence information of the two strands of DNA. Although not always expressed as blatantly, the intimate dependence of cellular function on the mechanical level of macromolecules is inspirational. The devil is in the structural detail, and the painstaking quest for the correct details and their returns in the form of reliable knowledge knows no shortcuts.