Experiments on mice show that TMC7, a transmembrane channel-like protein, localizes to the cis-Golgi region in spermatids and that this is essential for acrosome biogenesis and male fertility.

The structural relationship between TMC and TMEM16 proteins provides insight into the structure and functional mechanisms of the mechanotransduction channel complex in hair cells.

Complexes formed by calcium- and integrin-binding proteins 2 and 3 and transmembrane channel-like proteins 1 and 2 are essential for vertebrate hearing and balance and for fish lateral line function.

Other than its function in mechanotransduction, TMC1 is indispensable for action potential firing of auditory hair cells by mediating a leak conductance that alters tonotopically along the cochlea coil.

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.

Proteins in the Transmembrane Channel-Scramblase (TCS) superfamily share an evolutionarily conserved ability to permeate ions and phospholipids, challenging distinctions between ion channels and lipid scramblases.

Transcriptomic and genetic analyses of FoxO target genes reveal a key function of ER-associated protein degradation in growth regulation of Tsc1-deficient tissues.

Genetic deficits in auditory sensory transduction evoke changes in development and maturation of synapses between inner hair cells and spiral ganglion neurons, which can be partially recovered using inner ear gene therapy.

Tsc1 mutation in cerebellar Purkinje cells leads to downregulation of synapse genes that are targets of the Fragile X Mental Retardation Protein.

A set of ER-localized membrane proteins whose loss causes developmental diseases in humans, assemble with Sec61 into a translocon that facilitates the biogenesis of hundreds of different multi-pass membrane proteins.