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The Ca2+/calmodulin binding domain of the Ca2+-ATPase linked to the Na+,K+-ATPase alters transport stoichiometry

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Zhao,  Jianxing
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;
Shanghai Institute of Cell Biology, Chinese Academy of Sciences, 200031 Shanghai, China;

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Vasilets,  Larisa A.
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Chemical Physics, Russian Academy of Sciences, 142432 Chernogolovka, Russia;

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Yoshimura,  Shige H.
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;
Neurobiotechnology Center, Ohio State University, Columbus, OH 43210-1002, USA;
Faculty of Integrated Human Studies, Kyoto University, Kyoto 606-01, Japan;

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Gu,  Quanbao
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;
Shanghai Institute of Cell Biology, Chinese Academy of Sciences, 200031 Shanghai, China;

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Schwarz,  Wolfgang
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Zhao, J., Vasilets, L. A., Yoshimura, S. H., Gu, Q., Ishii, T., Takeyasu, K., et al. (1997). The Ca2+/calmodulin binding domain of the Ca2+-ATPase linked to the Na+,K+-ATPase alters transport stoichiometry. FEBS Letters, 408(3), 271-275. doi:10.1016/s0014-5793(97)00435-3.


Cite as: https://hdl.handle.net/21.11116/0000-0007-F86D-8
Abstract
Using Xenopus oocytes as an expression system, we have investigated ion-transport and ouabain-binding properties of a chimeric ATPase (alpha1-CBD; Ishii and Takeyasu (1995) EMBO J. 14, 58-67) formed by the alpha1-subunit of chicken Na+,K+-ATPase (alpha1) and the calmodulin binding domain (CBD) of the rat plasma membrane Ca2+-ATPase. alpha1-CBD can be expressed and transported to the oocyte plasma membrane without the beta-subunit, and shows ouabain binding. In contrast to ouabain binding, this chimera requires the beta-subunit for its cation (Na+ and K+) transport activity. alpha1-CBD exhibits an altered stoichiometry of Na+-K+ exchange. A detailed analysis of 22Na+ efflux, 86Rb+ uptake, pump current and ouabain binding suggests that the chimeric molecule can operate in an electrically silent 2Na+-2K+ exchange mode and, with much lower probability, in its normal 3Na+-2K+ exchange mode.