English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Background  The P-type ATPase family constitutes a collection of ion pumps that form phosphorylated intermediates during ion transport. One of the best known members of this family is the Na + ,K + -ATPase. The catalytic subunit of the Na + ,K + -ATPase includes several functional domains that determine its enzymatic and trafficking properties.    Methodology/Principal Findings  Using the yeast two-hybrid system we found that protein phosphatase 2A (PP2A) catalytic C-subunit is a specific Na + ,K + -ATPase interacting protein. PP-2A C-subunit interacted with the Na + ,K + -ATPase, but not with the homologous sequences of the H + ,K + -ATPase. We confirmed that the Na + ,K + -ATPase interacts with a complex of A- and C-subunits in native rat kidney. Arrestins and G-protein coupled receptor kinases (GRKs) are important regulators of G-protein coupled receptor (GPCR) signaling, and they also regulate Na + ,K + -ATPase trafficking through direct association. PP2A inhibits association between the Na + ,K + -ATPase and arrestin, and diminishes the effect of arrestin on Na + ,K + -ATPase trafficking. GRK phosphorylates the Na + ,K + -ATPase and PP2A can at least partially reverse this phosphorylation.    Conclusions/Significance  Taken together, these data demonstrate that the sodium pump belongs to a growing list of ion transport proteins that are regulated through direct interactions with the catalytic subunit of a protein phosphatase.

Protein Phosphatase 2A Interacts with the Na+,K+-ATPase and Modulates Its Trafficking by Inhibition of Its Association with Arrestin