Identification and Function of a Cytoplasmic K+ Site of the Na+, K+-ATPase
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چکیده
منابع مشابه
Identification of a pool of non-pumping Na/K-ATPase.
Recent studies have ascribed many non-pumping functions to the Na/K-ATPase. Here, we present experimental evidence demonstrating that over half of the plasma membrane Na/K-ATPase in LLC-PK1 cells is performing cellular functions other than ion pumping. This "non-pumping" pool of Na/K-ATPase, like the pumping pump, binds ouabain. Depletion of either cholesterol or caveolin-1 moves some of the "n...
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The Na/K-ATPase is a complex of integral membrane proteins that carries out active transport of sodium and potassium across the cell plasma membrane, and maintains chemical gradients of these ions. The alpha subunit of the Na/K-ATPase has several isoforms that are expressed in a cell type- and tissue-dependent manner. In adult vertebrates, while kidney cells express mostly alpha1, muscle and gl...
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1 A specific and essential role for Na,K-ATPase α3 in neurons co-expressing α1 and α3* Background: Neurons express two Na,K-ATPase isoforms, the ubiquitous α1 and neuron-specific α3. Result: α3 is important for control of membrane potential and is fully responsible for restoration of large [Na + ] i increases. Conclusion: α1 and α3 are required for basal neuronal function, but α3 controls resto...
متن کاملK+/Na+antagonism at cytoplasmic sites of Na+-K+-ATPase: a tissue-specific mechanism of sodium pump regulation.
Tissue-distinct interactions of the Na+-K+-ATPase with Na+ and K+, independent of isoform-specific properties, were reported previously (A. G. Therien, N. B. Nestor, W. J. Ball, and R. Blostein. J. Biol. Chem. 271: 7104-7112, 1996). In this paper, we describe a detailed analysis of tissue-specific kinetics particularly relevant to regulation of pump activity by intracellular K+, namely K+ inhib...
متن کاملIdentification of the 5-iodoacetamidofluorescein reporter site on the Na,K-ATPase.
5-Iodoacetamidofluorescein (5-IAF) labels the catalytic (alpha) subunit of dog kidney Na,K-ATPase without inhibiting enzymatic activity and is thus a useful fluorescent reporter of enzyme conformation under conditions of enzyme turnover. In this study conditions for labeling a unique sulfhydryl group are described, and this residue is identified in the cDNA-derived sequence. Reaction with iodoa...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2008
ISSN: 0021-9258
DOI: 10.1074/jbc.m803506200