Cargando…
Elevated intracellular Na(+) and osmolarity stimulate catalytic activity of the ubiquitin ligase Nedd4-2
Regulation of catalytic activity of E3 ubiquitin ligases is critical for their cellular functions. We identified an unexpected mode of regulation of E3 catalytic activity by ions and osmolarity; enzymatic activity of the HECT family E3 Nedd4-2/Nedd4L is enhanced by increased intracellular Na(+) ([Na...
Autores principales: | Persaud, Avinash, Jiang, Chong, Liu, Zetao, Kefalas, George, Demian, Wael L., Rotin, Daniela |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9335340/ https://www.ncbi.nlm.nih.gov/pubmed/35858421 http://dx.doi.org/10.1073/pnas.2122495119 |
Ejemplares similares
-
Comparison of substrate specificity of the ubiquitin ligases Nedd4 and Nedd4-2 using proteome arrays
por: Persaud, Avinash, et al.
Publicado: (2009) -
Rsp5/Nedd4 is the major ubiquitin ligase that targets cytosolic misfolded proteins upon heat-stress
por: Fang, Nancy N., et al.
Publicado: (2014) -
A Role for the Ubiquitin Ligase Nedd4 in Membrane Sorting of LAPTM4 Proteins
por: Milkereit, Ruth, et al.
Publicado: (2011) -
Regulation of the p38-MAPK pathway by hyperosmolarity and by WNK kinases
por: Liu, Zetao, et al.
Publicado: (2022) -
Transport of LAPTM5 to lysosomes requires association with the ubiquitin ligase Nedd4, but not LAPTM5 ubiquitination
por: Pak, Youngshil, et al.
Publicado: (2006)