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Structures of the signal recognition particle before and after it captures a transmembrane domain suggest how it chooses, engages, and shields its clients during membrane protein targeting to the endoplasmic reticulum.

A newly characterized calcium-activated chloride channel has been implicated in the immune system of Drosophila, shedding light on an enigmatic family of transmembrane proteins that are ubiquitous in nature.

A single transmembrane E3 ligase complex can regulate protein ubiquitination at multiple organelles using interchangeable targeting subunits.

Targeted mutations in a Ca²⁺-binding site of otoferlin, a transmembrane protein of synaptic vesicles defective in a recessive form of deafness, reveal its Ca²⁺ sensor role both for vesicle fusion and vesicle pool replenishment.

Chlamydia hijacks membrane trafficking proteins of the human host via the cytoplasmic domain of a secreted transmembrane protein.

A transmembrane protein uses distinct mechanisms to regulate the movement of specific toll-like receptors-key immune system components involved in detecting pathogens-to their final locations inside cells.

The coordination of protein targeting to the endoplasmic reticulum and the unfolded protein response through the stress sensor IRE1 ensures quality control of the secreted and transmembrane proteomes.

Genetic and functional studies reveal a previously unrecognized role for a transmembrane protein in glomerular filtration barrier function.

T antigen glycosylation, which marks metastatic cancer cells, is modulated on a small set of proteins by a conserved multipass transmembrane protein to allow tissue invasion by Drosophila macrophages.

Transmembrane protein 266 contains a functional S1-S4 voltage-sensing domain that is regulated by extracellular Zn²⁺ ions.