Assessment of GABARAP self-association by its diffusion properties
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- 作者：Victor Pacheco ; Peixiang Ma ; Yvonne Thielmann ; Rudolf Hartmann ; Oliver H. Weiergr?ber ; Jeannine Mohrl¨¹der and Dieter Willbold
- 关键词：Diffusion ; ordered spectroscopy ; NMR spectroscopy ; Protein oligomerization ; GABARAP
- 刊名：Journal of Biomolecular NMR
- 出版年：2010
- 出版时间：September 2010
- 年：2010
- 卷：48
- 期：1
- 页码：49-58
- 全文大小：490.9 KB
文摘
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 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.