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The cryo-EM structure of CRL7FBXW8 shows that CUL7–RBX1 binds FBXW8–SKP1 in an F-box-independent manner. Bridged by FBXW8–SKP1, CRL7FBXW8 forms a multi-cullin E3 ligase complex with neddylated CUL1–RBX1, which ubiquitinates a substrate recruited to CUL7.
The cryo-EM structures reveal orphan receptor GPR119 as the receptor for LPC. The structures with biochemical and functional data highlight evidence for LPC function in glucose regulation, and provide templates for drug design targeting GPR119.
A study published in Nature Structural & Molecular Biology now unveils, at the atomic level, the initial mechanisms of prion toxicity, providing insights into the pathogenic mechanisms of a protein neurodegenerative disease caused by protein misfolding.
CST is both an ssDNA-binding complex and a DNA Pol-α/primase cofactor that coordinates the switch from G-strand elongation to C-strand fill-in during telomere maintenance. Four papers in Nature Structural & Molecular Biology and Nature provide transformative insights into CST activity, providing a platform to understand lagging-strand synthesis genome wide.
Foutel et. al. identify conformational buffering as a mechanism for functional selection in intrinsically disordered protein regions that allows robust encoding of a tethering function by a hypervariable disordered linker through compensatory changes in sequence length and composition.
The H-latch is a well-defined structural change occurring in PrPC bound to the neurotoxic antibody POM1, and its presence shows a positive correlation with neurotoxicity. Inhibition of the H-latch prolongs the lifespan of prion-diseased mice.
Amplification of oncogene expression through extrachromosomal DNA is a common feature of many cancers and is associated with poor outcomes. Hung et al. review how regulation of extrachromosomal DNA gene expression is linked to alterations in chromatin structure and changes in contacts with DNA regulatory elements.
Elango et al. identify a new class of substrates on which the Fanconi anemia SLX4–XPF nuclease operates to mediate homologous recombination at DNA–protein replication fork barriers and promote cellular tolerance of DNA–protein cross-links.
An endogenous proteasome inhibitor was identified 30 years ago, but its mechanism remained unclear. Rawson et al. show that this inhibitor is present within the interior of the proteasome, where it simultaneously inhibits all six active sites.
Functional assays and cryo-EM structures show that ubiquitin binding and a cofactor drive protein quality-control client selection by the hybrid E2/E3 enzyme UBE2O.
Here, the authors find that histone demethylase Epe1-mediated stress resistance is regulated by proteasome-dependent truncation, allowing heterochromatin to reprogram gene expression that confers antifungal resistance to some fission yeast cells in the population.
Cryo-EM, X-ray crystallography and crosslinking mass spectrometry are harnessed to solve the structure of the full-length Rho-GEF P-Rex1, uncovering a two-layered mechanism of autoinhibition released upon Gβγ and PI(3,4,5)P3 binding.
This work reveals the structural and biochemical basis for phosphorylation-dependent day/night signaling by KaiC in the cyanobacterial circadian clock.
Clemons and colleagues identify a guided entry of tail-anchored proteins (GET) pathway in the pathogen Giardia intestinalis and characterize it structurally, revealing several previously unknown structures of the central protein Get3. The work resolves some important open questions and results in a comprehensive model for the insertion of tail-anchored membrane proteins.
Structural maintenance of chromosomes (SMC) complexes such as condensin regulate chromosome organization by extruding loops. A new study uses single-molecule imaging of condensin on supercoiled DNA to understand how condensins navigate the under- and overwound DNA states common throughout the genome.
Two new papers describe the successful purification of the partially intact human native red blood cell band 3 multiprotein membrane complexes, providing information that the authors then use to capture the structures and interactions of multiple erythrocyte proteins using high-resolution cryo-EM.
