Structural mapping of fluorescently-tagged, functional nhTMEM16 scramblase in a lipid bilayer.

ABSTRACT: Most members of the TransMEMbrane protein 16 (TMEM16) family are Ca²⁺-regulated scramblases that facilitate the bidirectional movement of phospholipids across membranes necessary for diverse physiological processes. The nhTMEM16 scramblase (from the fungus Nectria hematococca) is a homodimer with a large cytoplasmic region and a hydrophilic, membrane-exposed groove in each monomer. The groove provides the transbilayer conduit for lipids, but the mechanism by which Ca²⁺ regulates it is not clear. Because fusion of large protein tags at either the N or C terminus abolishes nhTMEM16 activity, we hypothesized that its cytoplasmic portion containing both termini may regulate lipid translocation via a Ca²⁺-dependent conformational change. To test this hypo

SUBMITTER: Andra KK 

PROVIDER: S-EPMC6078452 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature