Publications (15) View all
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Article: Structural characterization of intracellular C-terminal domains of group III metabotropic glutamate receptors.
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ABSTRACT: Metabotropic glutamate receptors (mGluRs) are regulated by interacting proteins that mostly bind to their intracellular C-termini. Here, we investigated if mGluR6, mGluR7a and mGluR8a C-termini form predefined binding surfaces or if they were rather unstructured. Limited tryptic digest of purified peptides argued against the formation of stable globular folds. Circular dichroism, (1)H NMR and (1)H(15)N HSQC spectra indicated the absence of rigid secondary structure elements. Furthermore, we localized short linear binding motifs in the unstructured receptor domains. Our data provide evidence that protein interactions of the analyzed mGluR C-termini are mediated rather by short linear motifs than by preformed folds.FEBS letters 02/2011; 585(3):511-6. · 3.54 Impact Factor -
Article: Preparation of a functional GABARAP-lipid conjugate in nanodiscs and its investigation by solution NMR spectroscopy.
ChemBioChem 09/2010; 11(14):1967-70. · 3.94 Impact Factor -
Article: Assessment of GABARAP self-association by its diffusion properties.
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ABSTRACT: Gamma-aminobutyric acid type A receptor-associated protein (GABARAP) belongs to a family of small ubiquitin-like adaptor proteins implicated in intracellular vesicle trafficking and autophagy. We have used diffusion-ordered nuclear magnetic resonance spectroscopy to study the temperature and concentration dependence of the diffusion properties of GABARAP. Our data suggest the presence of distinct conformational states and provide support for self-association of GABARAP molecules. Assuming a monomer-dimer equilibrium, a temperature-dependent dissociation constant could be derived. Based on a temperature series of (1)H(15)N heteronuclear single quantum coherence nuclear magnetic resonance spectra, we propose residues potentially involved in GABARAP self-interaction. The possible biological significance of these observations is discussed with respect to alternative scenarios of oligomerization.Journal of Biomolecular NMR 09/2010; 48(1):49-58. · 3.61 Impact Factor -
Article: Solution structure of Atg8 reveals conformational polymorphism of the N-terminal domain.
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ABSTRACT: During autophagy a crescent shaped like membrane is formed, which engulfs the material that is to be degraded. This membrane grows further until its edges fuse to form the double membrane covered autophagosome. Atg8 is a protein, which is required for this initial step of autophagy. Therefore, a multistage conjugation process of newly synthesized Atg8 to phosphatidylethanolamine is of critical importance. Here we present the high resolution structure of unprocessed Atg8 determined by nuclear magnetic resonance spectroscopy. Its C-terminal subdomain shows a well-defined ubiquitin-like fold with slightly elevated mobility in the pico- to nanosecond timescale as determined by heteronuclear NOE data. In comparison to unprocessed Atg8, cleaved Atg8(G116) shows a decreased mobility behaviour. The N-terminal domain adopts different conformations within the micro- to millisecond timescale. The possible biological relevance of the differences in dynamic behaviours between both subdomains as well as between the cleaved and uncleaved forms is discussed.Biochemical and Biophysical Research Communications 04/2010; 395(3):426-31. · 2.48 Impact Factor -
Article: Structure and potential function of gamma-aminobutyrate type A receptor-associated protein.
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ABSTRACT: The gamma-aminobutyrate type A receptor-associated protein (GABARAP) is a ubiquitin-like modifier, and is implicated in a variety of membrane trafficking and fusion events that are crucial to synaptic plasticity, autophagy and apoptosis. However, important aspects of GABARAP function and regulation remain poorly understood. We review the current state of knowledge about GABARAP, highlighting newly-identified GABARAP ligands, and discuss the possible physiological relevance of each ligand interaction.FEBS Journal 09/2009; 276(18):4989-5005. · 3.79 Impact Factor
