[ASAP] Programmed Allelic Mutagenesis of a DNA Polymerase with Single Amino Acid Resolution
June 29th, 2020 by
[ASAP] Physicochemical Tools for Visualizing and Quantifying Cell-Generated Forces
June 25th, 2020 by Ashley K. Nguyen and Kristopher A. Kilian*
Ubiquitination of interleukin-1{alpha} is associated with increased pro-inflammatory polarization of murine macrophages deficient in the E3 ligase ITCH [Cell Biology]
June 25th, 2020 by Xi Lin, Hengwei Zhang, Brendan F. Boyce, Lianping Xing
Macrophages play critical roles in homeostasis and inflammation. Macrophage polarization to either a pro-inflammatory or anti-inflammatory status is controlled by activating inflammatory signaling pathways. Ubiquitination is a post-translational modification that regulates these inflammatory signaling pathways. However, the influence of protein ubiquitination on macrophage polarization has not been well studied. We hypothesized that the ubiquitination status of key proteins in inflammatory pathways contributes to macrophage polarization, which is regulated by itchy E3 ubiquitin ligase (ITCH), a negative regulator of inflammation. Using ubiquitin proteomics, we found that ubiquitination profiles are different among polarized murine macrophage subsets. Interestingly, interleukin-1α (IL-1α), an important proinflammatory mediator, was specifically ubiquitinated in lipopolysaccharide-induced proinflammatory macrophages, which was enhanced in ITCH-deficient macrophages. The ITCH-deficient macrophages had increased levels of the mature form of IL-1α and exhibited proinflammatory polarization, and reduced deubiquitination of IL-1α protein. Finally, IL-1α neutralization attenuated pro-inflammatory polarization of the ITCH-deficient macrophages. In conclusion, ubiquitination of IL-1α is associated with increased pro-inflammatory polarization of macrophages deficient in the E3 ligase ITCH.Publisher Correction: Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family
June 25th, 2020 by Camila R. Santos
Nature Chemical Biology, Published online: 25 June 2020; doi:10.1038/s41589-020-0590-1
Publisher Correction: Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family[ASAP] Harnessing Natural Modularity of Metabolism with Goal Attainment Optimization to Design a Modular Chassis Cell for Production of Diverse Chemicals
June 22nd, 2020 by Sergio Garcia†‡ and Cong T. Trinh*†‡
[ASAP] Artificial Protein-Responsive Riboswitches Upregulate Non-AUG Translation Initiation in Yeast
June 22nd, 2020 by Fumihiro Horie, Kei Endo*, and Koichi Ito*
The uninhibited pathway is not worth studying
June 22nd, 2020 by Michael E. Pacold
Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0562-5
Glucose 6-phosphate dehydrogenase (G6PD) stands at the head of the pentose phosphate pathway, which is responsible for nucleotide synthesis. The identification and thorough validation of an improved G6PD inhibitor provide a valuable new tool compound for studying metabolism.Taking out the trash
June 22nd, 2020 by Grant Miura
Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0581-2
Taking out the trashDiscovering Nature’s super glue
June 22nd, 2020 by Zhi Zeng
Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0586-x
Molecular glues induce novel protein–protein interactions to modulate protein function and downstream biology. A recent study unveils manumycin polyketides with multiple electrophilic centers as covalent molecular glues between UBR7 and TP53.Spectroscopic coherent Raman imaging of <i>Caenorhabditis elegans</i> reveals lipid particle diversity
June 22nd, 2020 by Wei-Wen Chen
Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0565-2
A Raman-based imaging approach that can distinguish closely related chemical species used to characterize the distribution of lipids throughout the body of intact Caenorhabditis elegans worms shows that the epidermis is an important fat-storage reservoir.