Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
The mammalian mitochondrial transcription factor A (TFAM) is encoded in the nucleus and imported into mitochondria, where it functions as an activator of mtDNA transcription and packages mtDNA into DNA-protein aggregates called mitochondrial nucleoids. Two studies in this issue reveal that TFAM shapes mtDNA into a sharp U-turn, providing a molecular mechanism for its dual roles in the expression and maintenance of mtDNA.
The microRNA-induced silencing complex (miRISC) protein TNRC6 (also called GW182) uses dispersed tryptophan-containing repeats in unstructured regions to recruit the CCR4–NOT nuclease complex leading to mRNA deadenylation and inhibition of translation initiation according to new research.
One of the most versatile regulators of actin assembly, the WASP homology 2 (WH2) domain, reveals previously unknown facets by combining with a newly discovered actin-nucleating dimeric structure in the effector protein VopL from Vibrio parahaemolyticus.
Mechanistic details about complexin's contradictory double life as both a facilitator and an inhibitor of SNARE-mediated synaptic vesicle fusion have been challenging to uncover. A series of studies in this issue addresses the problem by revealing a switchable complexin conformation in which fusion arrest occurs when complexin clamps neighboring SNAREs.
The RING protein RBX-1 is implicated in both NEDDylation and ubiquitylation reactions. In this issue, new structural analysis reveals how conformational flexibility of the RBX-1 linker allows for a marked reorientation of the CUL1–RBX1 complex to facilitate transfer of NEDD8 or ubiquitin by closing the gap between the E2 catalytic site and the substrate.
The mechanisms of dynein activity have remained a mystery because of dynein's size and complexity, but two papers now shed light on how dynein functions at the molecular level.
A new study reveals that rewiring of MAPK signaling in cells expressing mutant RAS includes ERK-mediated BRAF inactivation and the concomitant activation of CRAF, partly through amplification by the phosphodiesterase 4 isoform.
In this issue, a wide array of structural and biochemical techniques are applied to reveal the molecular details of activity regulation in one of life's most essential enzymes, the ribonucleotide reductase.
Glutamate receptor ion channels use the free energy of ligand binding to trigger ion channel activation and desensitization. In this issue, an analysis of all-atom molecular dynamics simulations dissects the binding process, reveals a substantial gain in free energy produced by domain closure for agonists and reports unique energy landscapes for individual ligands.
Discrimination between self and non-self surfaces by the complement system of innate immunity has long been enigmatic. Finally, two papers provide structural insights into host protection against indiscriminate immune surveillance.
In this issue, two papers present contrasting models for the machinations of the measles virus attachment protein. Here we discuss how these reports illuminate possible intersubunit motions made by the protein as it drives the fusion of viral and cellular membranes during infection and further our understanding of this global scourge.
The interaction of autotaxin with its substrates leads to the production of lysophosphatidic acids (LPA), bioactive lipids with an emerging prominent role in inflammation and cancer. Two papers in this issue tell the previously unknown story of autotaxin, from substrate discrimination to highly efficient local delivery of LPA to target receptors.
