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• W2003661630 abstract "The proton pumping activity of the eukaryotic vacuolar ATPase (V-ATPase) is regulated by a unique mechanism that involves reversible enzyme dissociation. In yeast, under conditions of nutrient depletion, the soluble catalytic V₁ sector disengages from the membrane integral V_o, and at the same time, both functional units are silenced. Notably, during enzyme dissociation, a single V₁ subunit, C, is released into the cytosol. The affinities of the other V₁ and V_o subunits for subunit C are therefore of particular interest. The C subunit crystal structure shows that the subunit is elongated and dumbbell-shaped with two globular domains (C_head and C_foot) separated by a flexible helical neck region (Drory, O., Frolow, F., and Nelson, N. (2004) <i>EMBO Rep.</i> 5, 1148–1152). We have recently shown that subunit C is bound in the V₁-V_o interface where the subunit is in contact with two of the three peripheral stators (subunit EG heterodimers): one via C_head and one via C_foot (Zhang, Z., Zheng, Y., Mazon, H., Milgrom, E., Kitagawa, N., Kish-Trier, E., Heck, A. J., Kane, P. M., and Wilkens, S. (2008) <i>J. Biol. Chem.</i> 283, 35983–35995). <i>In vitro</i>, however, subunit C binds only one EG heterodimer (Féthière, J., Venzke, D., Madden, D. R., and Böttcher, B. (2005) <i>Biochemistry</i> 44, 15906–15914), implying that EG has different affinities for the two domains of the C subunit. To determine which subunit C domain binds EG with high affinity, we have generated C_head and C_foot and characterized their interaction with subunit EG heterodimer. Our findings indicate that the high affinity site for EGC interaction is C_head. In addition, we provide evidence that the EGC_head interaction greatly stabilizes EG heterodimer." @default.
• W2003661630 created "2016-06-24" @default.
• W2003661630 creator A5018158537 @default.
• W2003661630 creator A5043740049 @default.
• W2003661630 date "2010-08-01" @default.
• W2003661630 modified "2023-10-11" @default.
• W2003661630 title "Domain Characterization and Interaction of the Yeast Vacuolar ATPase Subunit C with the Peripheral Stator Stalk Subunits E and G" @default.
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• W2003661630 doi "https://doi.org/10.1074/jbc.m110.136960" @default.
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