IMR Press / FBL / Volume 10 / Issue 2 / DOI: 10.2741/1677

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Regions conferring isoform-specific function in the catalytic subunit of the Na,K-pump
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1 Department of Physiology, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA

Academic Editor: Joseph Shapiro

Front. Biosci. (Landmark Ed) 2005, 10(2), 2018–2026;
Published: 1 September 2005
(This article belongs to the Special Issue Regulation and function of NaK-ATPase in health and disease)

The Na,K-pump (i.e., Na,K-ATPase) is critical for maintaining the ionic gradients across the plasma membranes of animal cells. Its component subunits are expressed in multiple forms, but the physiological relevance of this subunit diversity remains unknown. The primary contributor to overall catalysis, the alpha subunit, exists in four isoforms. There are observed kinetic differences among these isoforms, but their subtlety makes them an unlikely basis for physiological significance. Instead, recent work suggests that the major functional distinction among the isoforms is their interaction with regulatory proteins. Moreover, the isoform-specific effects of modulatory agents such as protein kinase C seem to originate within two regions of structural divergence: the amino terminus and eleven residues near the center of the alpha subunit, the isoform-specific region.

Sequence comparisons
Structurefunction relationships
Protein kinase C
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