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| Home > Publications database > Assessment of GABARAP self-association by its diffusion properties |
| Journal Article | PreJuSER-14240 |
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2010
Springer Science + Business Media B.V
Dordrecht [u.a.]
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Please use a persistent id in citations: doi:10.1007/s10858-010-9437-5
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.
Keyword(s): Adaptor Proteins, Signal Transducing: chemistry (MeSH) ; Adaptor Proteins, Signal Transducing: metabolism (MeSH) ; Diffusion (MeSH) ; Humans (MeSH) ; Microtubule-Associated Proteins: chemistry (MeSH) ; Microtubule-Associated Proteins: metabolism (MeSH) ; Models, Molecular (MeSH) ; Nuclear Magnetic Resonance, Biomolecular: methods (MeSH) ; Protein Multimerization (MeSH) ; Temperature (MeSH) ; Adaptor Proteins, Signal Transducing ; GABARAP protein, human ; Microtubule-Associated Proteins ; J ; Diffusion-ordered spectroscopy (auto) ; NMR spectroscopy (auto) ; Protein oligomerization (auto) ; GABARAP (auto)
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