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.
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 region of the Biomphalaria genome, containing highly divergent haplotypes with different combinations of transmembrane genes, strongly impacts whether these snails can transmit parasitic schistosomes.