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Genetic screens and functional assays utilizing reporter mRNAs triggering NGD or COMD provide a basis for understanding the unique contributions of each pathway to translation-coupled mRNA decay and contextualizes their effects in the larger cellular process of translation surveillance.

To maintain the filtration barrier, slit diaphragms are cleansed by rapid cycles of raft-mediated endocytosis, while dynamin-dependent endocytosis prevents lateral diffusion of slit diaphragm protein.

Transferrin receptor 1-mediated iron uptake plays a pivotal role in osteoclast energy metabolism and cytoskeleton and regulates bone remodeling in female mice.

The active small G protein, Arl15-GTP, interacts with the MH2 domain of Smad4 and positively regulates the TGFß family signaling pathway by promoting the assembly of the Smad-complex.

Organ and vessel-type-specific differences in endothelial cell barrier composition and properties uncover the distinct importance of the major tight junction protein Claudin5 in restricting agonist-induced leakage.

A critical analysis of recent single-cell transcriptomic studies of Drosophila blood cells confirms the extreme plasticity of the major phagocyte class, identifies a new class of blood cell, and suggests relationships to blood cells in other insects.

Single-cell RNA-sequencing, spatial genomics, and histological analyses reveal that cold-induced brown adipose neogenesis is a complex adaptive response to elevated metabolic demand involving dynamic interactions between recruited immune cells and a subpopulation of poised adipocyte progenitors.

DIP2 is a conserved protein across fungi and animals that regulates specific diacylglycerol pools by diverting them to storage lipid biosynthesis to enable cellular homeostasis and adaptations.

Clathrin-coated vesicles can be made to form on intracellular membranes using a minimal molecular system, which defines the core vesicle budding machinery.

The ability of Vaccinia virus to induce actin polymerisation depends on the relative binding position of adaptors within the signalling network activating the Arp2/3 complex.