Cargando…
Phosphorylation of G3BP1-S149 does not influence stress granule assembly
Tourrière et al. (2003. J. Cell Biol. https://doi.org/10.1083/jcb.200212128) reported that G3BP1-S149 dephosphorylation promotes stress granule formation. We show that constructs used to establish this conclusion contain additional mutations causing these phenotypes, and that S149 phosphorylation st...
Autores principales: | Panas, Marc D., Kedersha, Nancy, Schulte, Tim, Branca, Rui M., Ivanov, Pavel, Anderson, Paul |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6605800/ https://www.ncbi.nlm.nih.gov/pubmed/31171631 http://dx.doi.org/10.1083/jcb.201801214 |
Ejemplares similares
-
Reply to “Phosphorylation of G3BP1-S149 does not influence stress granule assembly”
por: Tourrière, Hélène, et al.
Publicado: (2019) -
Viral and Cellular Proteins Containing FGDF Motifs Bind G3BP to Block Stress Granule Formation
por: Panas, Marc D., et al.
Publicado: (2015) -
G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits
por: Kedersha, Nancy, et al.
Publicado: (2016) -
Correction: G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits
por: Kedersha, Nancy, et al.
Publicado: (2019) -
The pseudophosphatase MK-STYX inhibits stress granule assembly independently of Ser149 phosphorylation of G3BP-1
por: Barr, Justinn E, et al.
Publicado: (2013)