Primate-specific isoform of Nedd4-1 regulates substrate binding via Ser/Thr phosphorylation and 14-3-3 binding
Abstract Nedd4 (Nedd4-1) is an E3 ubiquitin ligase involved in crucial biological processes such as growth factor receptor signaling. While canonical Nedd4-1 comprises a C2-WW(4)-HECT domain architecture, alternative splicing produces non-canonical isoforms that are poorly characterized. Here we cha...
Main Authors: | George Kefalas, Daniela Rotin |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2023-10-01
|
Series: | Scientific Reports |
Online Access: | https://doi.org/10.1038/s41598-023-44761-9 |
Similar Items
-
Deciphering the Arginine-binding preferences at the substrate-binding groove of Ser/Thr kinases by computational surface mapping.
by: Avraham Ben-Shimon, et al.
Published: (2011-11-01) -
Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms
by: Gergo Gogl, et al.
Published: (2021-03-01) -
Histone H3 Ser57 and Thr58 phosphorylation in the brain of 5XFAD mice
by: Kyle W. Anderson, et al.
Published: (2015-01-01) -
The peripheral binding of 14-3-3γ to membranes involves isoform-specific histidine residues.
by: Helene J Bustad, et al.
Published: (2012-01-01) -
Binding of the Human 14-3-3 Isoforms to Distinct Sites in the Leucine-Rich Repeat Kinase 2
by: Jascha T. Manschwetus, et al.
Published: (2020-04-01)