Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin

The mechanism by which Ser/Thr protein phosphatases specifically recruit and dephosphorylate their substrates is largely unclear. Hear, the authors elucidate how the Ser/Thr protein phosphatase calcineurin is recruited to its substrate NHE1 and how site-specific dephosphorylation is achieved.

Bibliographic Details
Main Authors: Ruth Hendus-Altenburger, Xinru Wang, Lise M. Sjøgaard-Frich, Elena Pedraz-Cuesta, Sarah R. Sheftic, Anne H. Bendsøe, Rebecca Page, Birthe B. Kragelund, Stine F. Pedersen, Wolfgang Peti
Format: Article
Language:English
Published: Nature Publishing Group 2019-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-11391-7
Description
Summary:The mechanism by which Ser/Thr protein phosphatases specifically recruit and dephosphorylate their substrates is largely unclear. Hear, the authors elucidate how the Ser/Thr protein phosphatase calcineurin is recruited to its substrate NHE1 and how site-specific dephosphorylation is achieved.
ISSN:2041-1723