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Disrupting the interaction between telomere protein TRF1 with meiosis-specific protein TERB1 impairs the pairing of X and Y chromosomes via their telomere-adjacent pseudoautosomal regions in pachytene, leading to spermatocyte apoptosis and male infertility in mice.
Structural and functional analyses of human TRF1 in complex with meiosis-specific protein TERB1 reveal the basis for telomere tethering to the inner nuclear membrane and offer insight into the mechanism of dissociation in late pachytene.
Abnormal pre-60S particles are able to escape nuclear quality control and join mature 40S subunits to catalyze cytoplasmic protein synthesis, but the resulting translation defects trigger the cytoplasmic surveillance machineries RQC and the Ski-exosome.
Biochemical and cellular analyses reveal that the helicase activity of DNA polymerase theta (Polθ) antagonizes RPA to promote DNA strand annealing and double-strand break repair via alt-NHEJ in mouse ES cells.
Biochemical reconstitution of PRC2 interactions with chromatinized templates demonstrates that protein-free linker DNA dominates the PRC2-nucleosome interaction, while RNA inhibits binding.
The crystal structure of the single-subunit oligosaccharyltransferase PglB in complex with acceptor peptide and a synthetic lipid-linked oligosaccharide analog reveals a key intermediate in the reaction mechanism.
CD28 signaling motifs are sequestered within the membrane via interactions with phospholipids. TCR activation increases the local Ca2+ concentration, which disrupts CD28-lipid interactions.
Histone H3 lysine 14 is propionylated and butyrylated in vivo in a metabolic-state-dependent manner and these modifications promote high levels of transcription.
This review highlights recent mechanistic insights into the CRISPR class 2 type V enzymes Cpf1 and C2c1, which are crucial for improving these genome engineering tools and expanding the genomic editing space.
Histone variant macroH2A1.1 inhibits PARP activity to maintain mitochondrial NAD+ pools in muscle cells, thus linking chromatin state to optimal energy metabolism.
Combined structural and microscopy approaches provide a model for how CAMSAP proteins recognize microtubule minus ends through their conserved CCK domains and protect microtubules from depolymerizing kinesin-13.
Analysis of the 3D genomic organization of Schizosaccharomyces pombe during the cell cycle reveals that condensin mediates formation of large domains that serve as chromosomal compaction units, whereas cohesin forms smaller, more stable domains.
Crystal structures and functional assays of a chimeric GABAA receptor in apo and pregnanolone-bound states reveal how neurosteroid binding alters receptor conformation to modulate channel opening.
PCSK9 enhances LDL cholesterol (LDL-c) levels by escorting the liver LDL receptor (LDLR) to endosomes and lysosomes for degradation. PCSK9 monoclonal antibodies and RNA-antisense formulations are effective in reducing LDL cholesterol in patients. The recent structural identification of a novel pocket in PCSK9 paves the way to the future development of orally active small-molecule hypocholesterolemic drugs.
The cellular crosstalk between different classes of regulatory noncoding RNAs has reached a new spatial dimension. Jiang et al. reveal an essential role of a nuclear-paraspeckle-organizing long noncoding RNA and its protein partners in regulating the first steps of microRNA biogenesis.
C-type inactivation is a process by which ion flux through a voltage-gated K+ channel is regulated at the selectivity filter. A recent structure of the Kv1.2 channel provides a view into the structural changes of the selectivity filter during C-type inactivation.
PERK is a major sensor of the unfolded protein response controlling cell fate under endoplasmic reticulum (ER) stress. A new study reveals an additional step for optimal PERK signaling, involving the binding of CNPY2 to PERK's luminal domain. The PERK–CNPY2 axis was shown to enhance cell death under ER stress in vivo influence liver disease.
Five protein complexes, CI–CV, form the oxidative phosphorylation electron transport chain in the mitochondrial membrane and can be found organized into supercomplexes (SCs): I+III2+IV, or respirasome; I+III2; III2+IV; and CV2. Letts and Sazanov review current knowledge on the structure, assembly and function of respiratory SCs.