SARS coronaviruses encode several mysterious proteins such as Orf3a and, in contrast to what has been claimed, Orf3a is not an ion channel but rather disrupts cellular trafficking by binding to the protein sorting complex known as HOPS.

Engineered E3 ubiquitin ligases are utilized to elucidate mechanisms underlying ubiquitin regulation of membrane proteins, and to achieve robust post-translational functional knockdown of ion channels.

Cytotoxicity associated with APOL1 renal-risk variants occurs through its plasma-membrane localization, where aberrant channel activity drives a sustained sodium and calcium influx leading to cell swelling and eventually cell death.

Hsp47 positively regulates the functional surface expression of endogenous GABA_A receptors and plays a critical and general role in the maturation of Cys-loop neuroreceptors.

Fatty acid analogues are interesting prototype compounds that may inspire the development of future I_Ks channel activators to treat patients with long QT syndrome caused by diverse arrhythmia-causing mutations in the I_Ks channel.

A cryo-EM structure of TMEM87A unexpectedly reveals it is structurally related to seven other proteins including Wntless, a chaperone for lipidated and secreted Wnt morphogens, suggesting GOLD-domain seven-transmembrane helix (GOST) proteins may all similarly traffic membrane-associated cargo.

Targeted recruitment of protein kinase A subunits enables distinctive regulation of the functional expression of a potassium channel depending on whether the enzyme is targeted to a pore-forming or auxiliary subunit.

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 functional interaction of Na⁺ and K_ATP channels at the intercalated disk of cardiomyocytes depends on Ankyrin G and is clinically relevant since K_ATP channel mutations affect Na⁺ channel expression.

By measuring the impacts of thousands of mutations on potassium channel trafficking and function, we illuminate the molecular basis of folding, structure–function relationships, and how these are altered in disease.