Contents
31 October 2017
Vol 10, Issue 503
Vol 10, Issue 503
Research Articles
- Endogenous retinoid X receptor ligands in mouse hematopoietic cells
The long-chain fatty acid C24:5 is likely an endogenous ligand of the retinoid X receptor α in mouse hematopoietic cells.
- MARK3-mediated phosphorylation of ARHGEF2 couples microtubules to the actin cytoskeleton to establish cell polarity
A phosphorylation switch releases sequestered ARHGEF2 from microtubules, enabling actin remodeling and formation of three-dimensional cell structures.
Research Resource
- Quantitative single-molecule imaging of TLR4 reveals ligand-specific receptor dimerization
Superresolution imaging of the pattern recognition receptor TLR4 reveals how different ligands control receptor dimerization.
Editors' Choice
- Endogenous defense against helminths
Secreted phospholipase A2 protects against helminth infection by damaging parasite larvae.
- Papers of note in Science 358 (6362)
This week’s articles describe how bacteria sense surfaces; the lysine acylation of host proteins mediated by a Vibrio cholerae toxin; and druggable proteases of malaria parasites.
- Papers of note in Science Translational Medicine 9 (413)
This week’s articles describe new therapeutic targets for pulmonary arterial hypertension, acute myeloid leukemia, and Friedreich’s ataxia.
- Papers of note in Science Immunology 2 (16)
This month’s articles show how type III interferons mediate antifungal immunity; examine the mechanism of lipid autoreactivity of T cell receptors; and implicate lysosomal signaling in controlling dendritic cell migration.
- Papers of note in Nature 550 (7677)
This week’s articles highlight inflammatory memory in epithelial stem cells; ubiquitin-specific protease inhibitors that target cancer cells; the identification of a sphingosine 1-phosphate exporter; and G protein signaling hotspots on the plasma membrane.
About The Cover
Online Cover This week features a Research Resource that reveals by superresolution imaging how different ligands control dimerization of the pattern recognition receptor TLR4. The image shows the crystal structure of mouse TLR4 in complex with its co-receptor MD-2 and the agonist LPS. [Image: PDB ID 3VQ2 visualized with the UCSF Chimera package]
