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Here the authors identify the transcription factors TFAP2C and TEAD4 as a bistable switch that reconciles into Hippo ON and OFF states, establishing a composite state at the eight-cell stage and critically regulating lineage diversification.
The authors solve a cryo-EM structure of the regulatory subunit of human protein phosphatase 2A in complex with HIV-1 Vif-containing E3 ligase, leading to improvement of our understanding of host–virus protein interactions.
Here the authors show that active DNA demethylation and transcription factor occupation at distal regulatory elements is essential for pluripotency maintenance in dormancy conditions.
Using time-resolved cryo-EM, the authors capture complete structural snapshots of the enzymatic cycle coupled with channel gating in a TRPM-type channel enzyme.
The authors revealed that the general translation factor eIF4A exerts a repressive effect on a subset of mRNAs by enhancing LARP1 and TOP mRNAs during mTORC1 inhibition under stress.
This study reports the structure of lysosomal N-acetyltransferase HGSNAT providing insights into the mechanism of lysosomal transmembrane acetylation of heparan sulfate required for its catabolism.
The authors identify genes potentially involved in NAD(H) redox modulation and provide insight on major hit HES4, which uses its transcriptional repressive function to drive pyrimidine nucleotide biosynthesis and tumor growth.
Here the authors used cryogenic electron microscopy and biochemistry to understand how yeast Mcm10 exerts its essential role in DNA replication initiation, finding that it splits the double Cdc45-MCM-GINS-Polε structure. The lagging-strand template is ejected from each MCM ring as the central channel of the helicase becomes too tight to accommodate two DNA strands.
Here, using cryo-EM, the authors reveal the mechanism by which RecA filamented on single-stranded DNA binds to and induces LexA cleavage, the key signal governing the bacterial DNA damage response pathway implicated in antibiotic resistance.
Designed novel protein nanoparticle technology integrates antibody targeting and responds to changes in environmental conditions to release protected molecular cargoes, opening new applications for precision medicine.
Telomeres are endogenous cellular targets of DNA ADP-ribosylation (DNA-ADPr). TARG1-regulated DNA-ADPr is coupled to lagging telomere DNA strand synthesis, and persistent DNA-ADPr, due to TARG1 deficiency, leads to telomere shortening and fragility.
The authors uncovered an antiparasitic molecule that exhibits broad-spectrum activity against parasitic flukes through engagement of a recently discovered transient receptor potential ion channel.
Using cryo-EM, the authors elucidate the mechanisms of TRPV1 regulation by bioactive lipids, namely phosphoinositides and the inflammatory lipid lysophosphatidic acid.
The antidepressant vortioxetine affects rodent and human 5-HT3 receptors differently. López-Sánchez et al. use a variety of methods, including structure determination of vortioxetine-bound human and mouse 5-HT3 receptors, to reveal the basis of these differences.
The authors used cryo-EM to visualize the arrangement of lipids at the closed groove of a TMEM16 scramblase and to reveal that both the structures and distributions of the protein’s conformations depend on the lipid composition and nanodisc scaffold.
The structures of the retrovirus-derived human syncytin-1 and suppressyn in complexes with their shared receptor reveal an ancient cellular recognition mechanism that underlies key morphological and immunological functions in placenta.
Chromatin condensation does not impede nucleosome sliding by ISWI remodelers. Notably, ATP energy is used not only for remodeling but also for enzyme mobility and to prevent solidification of chromatin. A ‘monkey-bar’ model rationalizes the findings.
In C. elegans, systemic RNAi is initiated by SID-1-mediated dsRNA internalization. Here the authors present cryo-EM structures of SID-1 homologs and the SID-1–dsRNA complex, elucidating the structural basis for dsRNA recognition and uptake by SID-1.
This study provides structural and biochemical insight into how mammalian PIWI proteins use a limited supply of piRNAs to silence a vast array of ever-evolving transposons in the germline.