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Opposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association

机译：肌醇六磷酸对棒抑制蛋白和抑制蛋白2自缔合的相反作用

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The robust cooperative formation of rod arrestin tetramers has been well-established, whereas the ability of other members of the arrestin family to self-associate remains controversial. Here, we used purified arrestins and multi-angle light scattering to quantitatively compare the propensity of the four mammalian arrestin subtypes to self-associate. Both non-visual and cone arrestins only form oligomers at very high non-physiological concentrations. However, inositol hexakisphosphate (IP6), a fairly abundant form of inositol in the cytoplasm, greatly facilitates self-association of arrestin2. Arrestin2 self-association equilibrium constants in the presence of 100 mu M IP6 suggest that an appreciable proportion could exist in an oligomeric state but only in intracellular compartments where its concentration is 5-10-fold higher than average. In contrast to arrestin2, IP6, inhibits self-association of rod arrestin, indicating that the structure of these two tetramers in solution is likely different.
机译：棒状阻滞蛋白四聚体的牢固的协同形成已被广泛确立，而抑制素家族的其他成员自我缔合的能力仍存在争议。在这里，我们使用纯化的抑制蛋白和多角度光散射来定量比较四种哺乳动物抑制蛋白亚型与自我缔合的倾向。非视觉和视锥蛋白都仅以非常高的非生理浓度形成寡聚物。但是，肌醇六磷酸（IP6）是细胞质中肌醇的一种相当丰富的形式，极大地促进了抑制蛋白2的自缔合。在100μMIP6存在下，arrestin2自缔合平衡常数表明，寡聚状态下可能存在相当比例，但仅存在于其浓度比平均值高5-10倍的细胞室内。与抑制蛋白2相比，IP6抑制杆抑制蛋白的自缔合，表明溶液中这两种四聚体的结构可能不同。

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