The range of molecular forms adopted by L1 retrotransposons reflect a tapestry of lifecycle-permissive and -restrictive host-parasite interactions occurring within cells.

Serine residues in proteins are the primary targets for PARP-dependent ADP-ribosylation signalling upon DNA damage.

Proteasomes are protected from autophagic elimination upon carbon starvation by sequestration into cytoplasmic storage granules, which aid cell fitness by providing a cache of proteasomes that can be rapidly remobilized when carbon availability improves.

Live-cell nanometer-resolution RNA labeling method enables transcriptome-wide mapping of endogenous RNAs in nuclear, cytosol, ER, and mitochondrial subcompartments.

The mechanism is revealed that connects the protein degradation machinery to cellular membrane-bound compartments during proteostasis stress in mammalian cells.

Ser57 phosphorylation regulates ubiquitin homeostasis by inhibiting deubiquitylase-mediated recycling and promoting vacuolar degradation.

A detailed analysis of protein abundance and phosphorylation changes across mitotic subphases and interphase in asynchronously growing human cells has been enabled by combining FACS with quantitative MS-based proteomics.

The ER membrane protein complex promotes the biogenesis of a subset multipass membrane proteins enriched for transporters and other proteins with destabilizing features in transmembrane domains.

Thalidomide and its derivates induce degradation of many C₂H₂ zinc-finger transcription factors, including SALL4, providing insight into a long-standing mystery in modern pharmacology, and starting points for future drug development.

AurkA is imported into mitochondria at interphase, and it induces organelle elongation and enhances ATP production when over-expressed.