The placement of single methyl groups at certain positions in the sequence of small model transmembrane proteins consisting solely of leucines and isoleucines can modulate highly specific, productive interactions with the transmembrane domain of the erythropoietin receptor.
Diverse biophysical properties of β1 and β3 integrin transmembrane and cytoplasmic domains result in distinct mechanisms of integrin activation and function.
Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.
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.
A zebrafish model for a particular form of human deafness (DFNB63) changes our view of this disease by revealing a defect in the localization of Transmembrane channel-like proteins that are essential for mechanotransduction in sensory cells.
A small molecule, cotransin, blocks transmembrane domains form integrating into cell membranes by allosterically ‘locking’ the lateral gate of the Sec61 translocation channel.
A membrane protein complex in the endoplasmic reticulum is a key factor for the biogenesis of multi-pass transmembrane proteins, including Rh1, and its loss causes retinal degeneration.
A region of the Biomphalaria genome, containing highly divergent haplotypes with different combinations of transmembrane genes, strongly impacts whether these snails can transmit parasitic schistosomes.
