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.
Guardado en:
Autores principales: | 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 |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/5e565aa376cd44bab46f43a617043caa |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Structural basis of response regulator dephosphorylation by Rap phosphatases.
por: Vijay Parashar, et al.
Publicado: (2011) -
Old and New Calcineurin Inhibitors in Lupus Nephritis
por: Claudio Ponticelli, et al.
Publicado: (2021) -
Decreased calcineurin immunoreactivity in the postmortem brain of a patient with schizophrenia who had been prescribed the calcineurin inhibitor, tacrolimus, for leukemia
por: Wada A, et al.
Publicado: (2016) -
A Review of Calcineurin Biophysics with Implications for Cardiac Physiology
por: Ryan B. Williams, et al.
Publicado: (2021) -
Dephosphorylated parafibromin is a transcriptional coactivator of the Wnt/Hedgehog/Notch pathways
por: Ippei Kikuchi, et al.
Publicado: (2016)