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.
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.
The host transmembrane protein MARCH8, previously known as an expression regulator of host proteins, is a powerful antiviral host factor with a potentially broad antiviral spectrum through two different mechanisms.
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.
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.