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.
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.
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.
Inhibition of C. elegans FLD-1 or Human TLCD1/2 prevents saturated fat lipotoxicity by allowing increased levels of membrane phospholipids that contain fluidizing long-chain polyunsaturated fatty acids.
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.
First two transmembrane segments of Tim17 are involved in interaction with the channel and the second two with the motor of the presequence translocase suggesting how proteins are handed over during their translocation into mitochondria.