Membrane trafficking articles from across Nature Portfolio

We introduce lipid-trap mass spectrometry (LTMS), a technique to systematically identify lipid–protein interactions directly captured from live mammalian cells. By applying LTMS to proteins associated with the cell membrane during cytokinesis, we revealed that proteins bind specific lipid species, which suggests that membrane proteins function in selective lipid nanoenvironments.

This study characterizes a specialized chloroplast membrane subdomain that includes lipid transporters and thylakoid biogenesis machinery. Novel candidate proteins regulate thylakoid membrane architecture essential for plant photosynthesis.

The mechanisms of collagen export from the ER are poorly understood. Here, the authors show that collagen transport initiation induces site-specific O-GlcNAcylation of the COPII protein Sec24D, remodeling its interactome and facilitating trafficking.

The ESCRT-protein HRS undergoes two-dimensional phase separation on endosomal membranes to form gel-like condensates that recruit clathrin into multilayered, flat coats. Cholesterol enhances this process and drives stable cargo-sorting microdomains

Here the authors show that inhibition of host N-myristoyltransferase by IMP1088 reduces SARS-CoV-2, VSV and RSV infection across lung and nasal cells, through a Golgi-bypassing virion egress that disrupts spike maturation and yields less infectious progeny, supporting host-directed antivirals.

Germ granule components maintain protein levels of endolysosomal components via small RNA-mediated regulation during the oocyte-to-embryo transition, thereby ensuring spatiotemporal endosomal activation (endosomal switching) for proper embryogenesis.

Cell migration depends on controlled adhesion turnover, but its regulation remains unclear. Here the authors show that AAK1 promotes focal adhesion disassembly via PDLIM5 and Talin1 phosphorylation, enabling efficient cell migration.

We introduce lipid-trap mass spectrometry (LTMS), a technique to systematically identify lipid–protein interactions directly captured from live mammalian cells. By applying LTMS to proteins associated with the cell membrane during cytokinesis, we revealed that proteins bind specific lipid species, which suggests that membrane proteins function in selective lipid nanoenvironments.

Damaged mitochondria must be removed to preserve organelle function, and a quality control pathway segregates damaged peripheral subdomains into small MTFP1-enriched mitochondria targeted for degradation. A study now identifies MISO as the key factor that promotes subdomain formation and links mitochondrial dynamics, quality control and mtDNA homeostasis.