Target of rapamycin FATC domain as a general membrane anchor: The FKBP-12 like domain of FKBP38 as a case study.

ABSTRACT: Increased efforts have been undertaken to better understand the formation of signaling complexes at cellular membranes. Since the preparation of proteins containing a transmembrane domain or a prenylation motif is generally challenging an alternative membrane anchoring unit that is easy to attach, water-soluble and binds to different membrane mimetics would find broad application. The 33-residue long FATC domain of yeast TOR1 (y1fatc) fulfills these criteria and binds to neutral and negatively charged micelles, bicelles, and liposomes. As a case study, we fused it to the FKBP506-binding region of the protein FKBP38 (FKBP38-BD) and used ¹ H-¹⁵ N NMR spectroscopy to characterize localization of the chimeric protein to micelles, bicelles, and liposomes. Based on these an

SUBMITTER: De Cicco M 

PROVIDER: S-EPMC5775168 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature