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Structure-function relations of interactions between Na,K-ATPase, the gamma subunit, and corticosteroid hormone-induced factor.

Authors: Lindzen, M  Aizman, R  Lifshitz, Y  Lubarski, I  Karlish, SJ  Garty, H 
Citation: Lindzen M, etal., J Biol Chem. 2003 May 23;278(21):18738-43. Epub 2003 Mar 7.
Pubmed: (View Article at PubMed) PMID:12626497
DOI: Full-text: DOI:10.1074/jbc.M213253200

Corticosteroid hormone-induced factor (CHIF) and the gamma subunit of the Na,K-ATPase (gamma) are two members of the FXYD family whose function has been elucidated recently. CHIF and gamma interact with the Na+ pump and alter its kinetic properties, in different ways, which appear to serve their specific physiological roles. Although functional interactions with the Na,K-ATPase have been clearly demonstrated, it is not known which domains and which residues interact with the alpha and/or beta subunits and affect the pump kinetics. The current study provides the first systematic analysis of structure-function relations of CHIF and gamma. It is demonstrated that the stability of detergent-solubilized complexes of CHIF and gamma with alpha and/or beta subunits is determined by the trans-membrane segments, especially three residues that may be involved in hydrophobic interactions. The transmembrane segments also determine the opposite effects of CHIF and gamma on the Na+ affinity of the pump, but the amino acids involved in this functional effect are different from those responsible for stable interactions with alpha.


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CRRD Object Information
CRRD ID: 1598991
Created: 2007-01-10
Species: All species
Last Modified: 2007-01-10
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.