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.
The structure of a bivalent double-knot tarantula toxin bound to the outer pore of the capsaicin receptor reveals a novel mode of toxin-channel recognition that has important implications for thermosensation.
Independently gating ion channels typically act fast within milliseconds, but cooperative interactions within a cluster of channels allow for a memory of previous electrical activity for several seconds.
Computation and experiment together demonstrate that nonspecific membrane–protein interactions could regulate transmembrane protein function and suggest that covalent linkers can be an integral component of the sensing apparatus.
A single-nucleotide I232T polymorphic change in FcγRIIB's transmembrane domain bends FcγRIIB's ectodomains toward cell membrane to allosterically hinder FcγRIIB's ligand association, providing novel molecular mechanism for functional loss of FcγRIIB-I232T.