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Imaging, quantitative immunoblotting and mass spectrometry reveal that hundreds of surface-expressed neuronal membrane proteins exhibit atypical glycosylation profiles, resulting in changes in protein half-life and synaptic responses.

The ERK8 kinase blocks the export of glycosyl-tranferases from the Golgi to the endoplasmic reticulum, and thus subsequent O-glycosylation of proteins that otherwise enhance cell motility and tissue invasion.

The soluble cargo protein albumin traverses the Golgi stack at much faster rates than procollagen aggregates, by diffusion via intercisternal continuities.

A zebrafish model for a particular form of human deafness (DFNB63) changes our view of this disease by revealing a defect in the localization of Transmembrane channel-like proteins that are essential for mechanotransduction in sensory cells.

Plasticity arising from autocatalytic receptor activation coexists with robustness in ligand responsiveness only by differential endosomal sorting of spontaneous and ligand-activated EGFR as distinct molecular states.

Emerin, a protein that plays key roles in nuclear organization, can be dynamically degraded in response to environmental stimuli such as ER stress.

The iRhom2 protein, a catalytically inactive relative of rhomboid proteases, controls inflammation and growth factor signalling by acting as an essential multifunctional regulatory subunit of the cell surface shedding protease TACE (ADAM17).

The association of caveolin with the potassium channel Kv1.3 fine-tunes cell survival and apoptosis.

HiLITR is a molecular reporter of protein localization that enables straightforward, large-scale, fluorescence-activated cell sorting-based discovery of genes that regulate complex cellular processes, such as mitochondrial and ER tail-anchored protein trafficking.

An endoplasmic reticulum membrane protein regulates synaptic transmission, alcohol sensitivity, and gene expression by controlling the trafficking of a calcium-activated potassium channel.