Structural flexibility of the synaptobrevin-2 transmembrane domain promotes membrane fusion.

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.

Designer transmembrane peptides precisely control chimeric antigen receptor signaling strength and are insulated from undesired interactions with endogenous receptors.

Structure-based alignment of TRP channels enables comparison of structural changes, ion permeation pathways and ligand-binding sites and reveals over-representation of structures that represent non-conducting states.

Diverse biophysical properties of β1 and β3 integrin transmembrane and cytoplasmic domains result in distinct mechanisms of integrin activation and function.

Single molecule subunit counting, FRET and electrophysiology experiments reveal that metabotropic glutamate receptor subunits interact and rearrange at the level of the transmembrane domains in response to allosteric modulators.

A widespread family of chaperones functions to stabilize membrane protein effectors by mimicking transmembrane helical environments and promotes effector export by the bacterial type VI secretion system.

Homo- and heterodimeric group II metabotropic glutamate receptors show diverse modes of interaction between transmembrane domains that control their distinct assembly and activation properties.

Naturally-occurring v-SNARE TMD variants differentially regulate fusion pore dynamics and cooperate with phospholipids in supporting membrane curvature at the fusion pore neck.

A new insight into the role of syntaxin1's juxtamembrane region in controlling palmitoylation and spontaneous neurotransmitter release.