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Specialized Functional Diversity and Interactions of the Na,K-ATPase

Na,K-ATPase is a protein ubiquitously expressed in the plasma membrane of all animal cells and vitally essential for their functions. A specialized functional diversity of the Na,K-ATPase isozymes is provided by molecular heterogeneity, distinct subcellular localizations, and functional interactions...

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Autores principales: Matchkov, Vladimir V., Krivoi, Igor I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4879863/
https://www.ncbi.nlm.nih.gov/pubmed/27252653
http://dx.doi.org/10.3389/fphys.2016.00179
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author Matchkov, Vladimir V.
Krivoi, Igor I.
author_facet Matchkov, Vladimir V.
Krivoi, Igor I.
author_sort Matchkov, Vladimir V.
collection PubMed
description Na,K-ATPase is a protein ubiquitously expressed in the plasma membrane of all animal cells and vitally essential for their functions. A specialized functional diversity of the Na,K-ATPase isozymes is provided by molecular heterogeneity, distinct subcellular localizations, and functional interactions with molecular environment. Studies over the last decades clearly demonstrated complex and isoform-specific reciprocal functional interactions between the Na,K-ATPase and neighboring proteins and lipids. These interactions are enabled by a spatially restricted ion homeostasis, direct protein-protein/lipid interactions, and protein kinase signaling pathways. In addition to its “classical” function in ion translocation, the Na,K-ATPase is now considered as one of the most important signaling molecules in neuronal, epithelial, skeletal, cardiac and vascular tissues. Accordingly, the Na,K-ATPase forms specialized sub-cellular multimolecular microdomains which act as receptors to circulating endogenous cardiotonic steroids (CTS) triggering a number of signaling pathways. Changes in these endogenous cardiotonic steroid levels and initiated signaling responses have significant adaptive values for tissues and whole organisms under numerous physiological and pathophysiological conditions. This review discusses recent progress in the studies of functional interactions between the Na,K-ATPase and molecular microenvironment, the Na,K-ATPase-dependent signaling pathways and their significance for diversity of cell function.
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spelling pubmed-48798632016-06-01 Specialized Functional Diversity and Interactions of the Na,K-ATPase Matchkov, Vladimir V. Krivoi, Igor I. Front Physiol Physiology Na,K-ATPase is a protein ubiquitously expressed in the plasma membrane of all animal cells and vitally essential for their functions. A specialized functional diversity of the Na,K-ATPase isozymes is provided by molecular heterogeneity, distinct subcellular localizations, and functional interactions with molecular environment. Studies over the last decades clearly demonstrated complex and isoform-specific reciprocal functional interactions between the Na,K-ATPase and neighboring proteins and lipids. These interactions are enabled by a spatially restricted ion homeostasis, direct protein-protein/lipid interactions, and protein kinase signaling pathways. In addition to its “classical” function in ion translocation, the Na,K-ATPase is now considered as one of the most important signaling molecules in neuronal, epithelial, skeletal, cardiac and vascular tissues. Accordingly, the Na,K-ATPase forms specialized sub-cellular multimolecular microdomains which act as receptors to circulating endogenous cardiotonic steroids (CTS) triggering a number of signaling pathways. Changes in these endogenous cardiotonic steroid levels and initiated signaling responses have significant adaptive values for tissues and whole organisms under numerous physiological and pathophysiological conditions. This review discusses recent progress in the studies of functional interactions between the Na,K-ATPase and molecular microenvironment, the Na,K-ATPase-dependent signaling pathways and their significance for diversity of cell function. Frontiers Media S.A. 2016-05-25 /pmc/articles/PMC4879863/ /pubmed/27252653 http://dx.doi.org/10.3389/fphys.2016.00179 Text en Copyright © 2016 Matchkov and Krivoi. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Matchkov, Vladimir V.
Krivoi, Igor I.
Specialized Functional Diversity and Interactions of the Na,K-ATPase
title Specialized Functional Diversity and Interactions of the Na,K-ATPase
title_full Specialized Functional Diversity and Interactions of the Na,K-ATPase
title_fullStr Specialized Functional Diversity and Interactions of the Na,K-ATPase
title_full_unstemmed Specialized Functional Diversity and Interactions of the Na,K-ATPase
title_short Specialized Functional Diversity and Interactions of the Na,K-ATPase
title_sort specialized functional diversity and interactions of the na,k-atpase
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4879863/
https://www.ncbi.nlm.nih.gov/pubmed/27252653
http://dx.doi.org/10.3389/fphys.2016.00179
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