[NMR paper] NMR- and CD-Monitored Lipid-Binding Studies Suggest a General Role for the FATC Domain as Membrane Anchor of Phosphatidyl-Inositol-3 Kinase-Related Kinases (PIKKs).
NMR- and CD-Monitored Lipid-Binding Studies Suggest a General Role for the FATC Domain as Membrane Anchor of Phosphatidyl-Inositol-3 Kinase-Related Kinases (PIKKs).
Related ArticlesNMR- and CD-Monitored Lipid-Binding Studies Suggest a General Role for the FATC Domain as Membrane Anchor of Phosphatidyl-Inositol-3 Kinase-Related Kinases (PIKKs).
J Biol Chem. 2013 May 13;
Authors: Sommer LA, Schaad M, Dames SA
Abstract
The FATC domain is shared by all members of the family of phosphatidylinositol-3 kinase related kinases (PIKKs). It has been shown that the FATC domain plays an important role for the regulation of each PIKK. However, besides an involvement in protein-protein interactions a common principle for the action of the FATC domain has not been detected. A detailed characterization of the structure and lipid-binding properties of the FATC domain of the ser/thr kinase target of rapamycin (TOR) revealed that it contains a redox-sensitive membrane anchor in its C-terminus. Since the C-terminal regions of the FATC domains of all known PIKKs are rather hydrophobic and especially rich in aromatic residues, we analyzed if the ability to interact with lipids and membranes may be a general property. Here, we present the characterization of the interactions with lipids and different membrane-mimetics for the FATC domains of human DNA-PKcs, human ATM, human ATR, human SMG-1, and human TRRAP by NMR and CD spectroscopy. The data indicate that all can interact with different membrane-mimetics and only may have different preferences for membrane properties such as surface charge, curvature, and lipid packing. The oxidized form of the TOR FATC domain is overall well structured and forms an ?-helix that is followed by a disulfide-bonded loop. In contrast, the FATC domains of the other PIKKs are rather unstructured in the isolated form and only significantly populate ?-helical secondary structure upon interacting with membrane-mimetics.
PMID: 23671275 [PubMed - as supplied by publisher]
Determination of the Lithium Binding Site in Inositol Monophosphatase, the Putative Target for Lithium Therapy, by Magic-Angle-Spinning Solid-State NMR
Determination of the Lithium Binding Site in Inositol Monophosphatase, the Putative Target for Lithium Therapy, by Magic-Angle-Spinning Solid-State NMR
Anat Haimovich, Uzi Eliav and Amir Goldbourt
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja211794x/aop/images/medium/ja-2011-11794x_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja211794x
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/zT_WbDH70WA
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Virol J. 2010 Dec 31;7(1):379
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Multidimensional heteronuclear NMR techniques were applied to study the phosphotransfer domain,...
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The...
NMR- and CD-Monitored Lipid-Binding Studies Suggest a General Role for the FATC Domain as Membrane Anchor of Phosphatidyl-Inositol-3 Kinase-Related Kinases (PIKKs).
Linear Mode
