The cryo-EM structure of the human transcription-export THO–UAP56 complex reveals mechanisms of mRNA nuclear export licensing.

Prokaryotes use polycistronic messages for coordinated translation, whereas eukaryotic cells may achieve tunable protein synthesis by packaging monocistronic mRNAs into functional multiplexes via co-transcriptional interallelic coupling and non-canonical histone-H4 functions.

The packaging signal in HIV-1 genomic RNA supports in vitro particle assembly more efficiently than control RNAs, probably explaining its selective packaging during virus assembly in vivo.

Ribosomal profiling reveals that translational repression is an important mechanism for cell cycle control and can complement protein degradation.

Cryo-electron tomography unveils striking new structural components of positive-strand virus RNA replication compartments, greatly advancing mechanistic insights into the structure, assembly, function and control of these critical complexes.

Mitochondria serve as a reservoir for the sorting of an miRNA into P-bodies and from there into exosomes secreted from human cultured cells.

An NMR-based structural study of sperm proteins reveals a novel protein packaging/dispersion system embedded in a coevolutionary arms race.

COPII vesicles regulate the metabolism of cholesterol through the selective transport of secretory proteins.

Structural, biochemical, and proteomic analyses of a four-subunit core module of the cleavage and polyadenylation specificity factor complex reveal its molecular architecture and specific determinants of polyadenylation signal recognition in human mRNAs.

Quantitative super resolution imaging, in live mammalian cells, reveals a direct relationship between protein clustering dynamics and the number of mRNA transcribed at an endogenous gene locus.