Is the C-terminal arm of lens gap junction channel protein the channel gate?

Abstract

Lens gap junction channels are studied in a reconstituted system obtained by incorporating into liposomes, with or without calmodulin, the lens junction protein (MIP26) and its trypsin-cleaved product (MIP21) that lacks the C-terminal arm. Channel permeability is studied with an osmotic swelling assay. MIP26 and MIP21 liposomes swell in sucrose or polyethyleneglycol with or without Ca ++ indicating the presence of large channels. Without Ca ++, MIP26 and MIP21 liposomes swell in both permeants. With Ca ++, MIP26-calmodulin liposomes do not swell in either permeant, indicating complete channel closure, while MIP21-calmodulin liposomes swell in sucrose but not in polyethyleneglycol. This suggests that the C-terminal arm participates in channel gating.