Structural basis of Ca²⁺-dependent activation and lipid transport by a TMEM16 scramblase.

ABSTRACT: The lipid distribution of plasma membranes of eukaryotic cells is asymmetric and phospholipid scramblases disrupt this asymmetry by mediating the rapid, nonselective transport of lipids down their concentration gradients. As a result, phosphatidylserine is exposed to the outer leaflet of membrane, an important step in extracellular signaling networks controlling processes such as apoptosis, blood coagulation, membrane fusion and repair. Several TMEM16 family members have been identified as Ca²⁺-activated scramblases, but the mechanisms underlying their Ca²⁺-dependent gating and their effects on the surrounding lipid bilayer remain poorly understood. Here, we describe three high-resolution cryo-electron microscopy structures of a fungal scramblase from Aspergillus f

SUBMITTER: Falzone ME 

PROVIDER: S-EPMC6355197 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature