Structural basis for the association of the redox-sensitive target of rapamycin FATC domain with membrane-mimetic micelles.

ABSTRACT: The target of rapamycin (TOR) is a conserved eukaryotic Ser/Thr kinase that regulates cellular growth in response to the nutrient and energy state. TOR signaling plays an important role in the development of diseases such as cancer, obesity, and diabetes and in different redox-sensitive processes (hypoxia, apoptosis, and aging). Because TOR has been detected at different cellular membranes and in the nucleus, its localization may influence the specific signaling readout. To better understand how TOR can associate with different membranes, the lipid-binding properties of the redox-sensitive yeast TOR1 FATC domain (y1fatc) have been characterized by solution NMR spectroscopy. Binding studies with different lipids indicate that y1fatc interacts specifically with a membrane-mimetic environment

SUBMITTER: Dames SA 

PROVIDER: S-EPMC2844220 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature