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Sommer, L.A.* ; Dames, S.A.

Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.

FEBS Lett. 588, 1755-1766 (2014)
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The conserved C-terminal FATC domain of the kinase 'target of rapamycin' is important for its regulation and was suggested to contain a peripheral membrane anchor. Here, we present the characterization of the interactions of the yeast TOR1 FATC domain (2438-2470 = y1fatc) and 15 mutants with membrane mimetic micelles, bicelles, and small unilamellar vesicles (SUVs) by NMR and CD spectroscopy. Replacement of up to 6-7 residues did not result in a significant abrogation of the association with micelles or bicelles. However, replacement of only one residue could result in an impairment of the interaction with SUVs that are usually used at low concentrations. Some mutants not binding liposomes may be introduced in full-length TOR for future functional and localization studies in vivo.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Bicelle ; Cd ; Kinase ; Liposome ; Membrane Mimetic ; Micelle ; Nmr ; Protein Lipid Interactions ; Protein Membrane Interactions ; Suv ; Target Of Rapamycin; Mammalian Target; Endoplasmic-reticulum; Binding Domain; Saccharomyces-cerevisiae; 3-dimensional Structure; Phosphatidic-acid; Growth-control; Lipid-binding; Localization; Complex
Sprache englisch
Veröffentlichungsjahr 2014
HGF-Berichtsjahr 2014
ISSN (print) / ISBN 0014-5793
e-ISSN 1873-3468
Zeitschrift FEBS Letters
Quellenangaben Band: 588, Heft: 9, Seiten: 1755-1766 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort Amsterdam
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
POF Topic(s) 30505 - New Technologies for Biomedical Discoveries
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-503000-006
PubMed ID 24704685
DOI 10.1016/j.febslet.2014.03.031
WOS ID WOS:000335450200039
Scopus ID 84899652396
Erfassungsdatum 2014-04-09
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