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 monomerâ??dimer equilibrium, a temperature-dependent dissociation constant could be derived. Based on a temperature series of 1H15N 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.
- Content Type Journal Article
- DOI 10.1007/s10858-010-9437-5
- Authors
- Victor Pacheco, Forschungszentrum Jülich Institut für Strukturbiologie und Biophysik 3 52425 Jülich Germany
- Peixiang Ma, Forschungszentrum Jülich Institut für Strukturbiologie und Biophysik 3 52425 Jülich Germany
- Yvonne Thielmann, Forschungszentrum Jülich Institut für Strukturbiologie und Biophysik 3 52425 Jülich Germany
- Rudolf Hartmann, Forschungszentrum Jülich Institut für Strukturbiologie und Biophysik 3 52425 Jülich Germany
- Oliver H. Weiergräber, Forschungszentrum Jülich Institut für Strukturbiologie und Biophysik 2 52425 Jülich Germany
- Jeannine Mohrlüder, Forschungszentrum Jülich Institut für Strukturbiologie und Biophysik 3 52425 Jülich Germany
- Dieter Willbold, Forschungszentrum Jülich Institut für Strukturbiologie und Biophysik 3 52425 Jülich Germany
Source: Journal of Biomolecular NMR