Cargando…
EGFR-dependent tyrosine phosphorylation of integrin β4 is not required for downstream signaling events in cancer cell lines
In epithelial cancers, the epidermal growth factor receptor (EGFR) and integrin α6β4 are frequently overexpressed and found to synergistically activate intracellular signaling pathways that promote cell proliferation and migration. In cancer cells, the β4 subunit is phosphorylated at tyrosine residu...
Autores principales: | te Molder, Lisa, Kreft, Maaike, Heemskerk, Niels, Schuring, Joyce, de Pereda, Jose M., Wilhelmsen, Kevin, Sonnenberg, Arnoud |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8060419/ https://www.ncbi.nlm.nih.gov/pubmed/33883672 http://dx.doi.org/10.1038/s41598-021-88134-6 |
Ejemplares similares
-
PKD2 and RSK1 Regulate Integrin β4 Phosphorylation at Threonine 1736
por: te Molder, Lisa, et al.
Publicado: (2015) -
Comparative interactomics analysis reveals potential regulators of α6β4 distribution in keratinocytes
por: te Molder, Lisa, et al.
Publicado: (2020) -
Kindlin-1 Regulates Integrin Dynamics and Adhesion Turnover
por: Margadant, Coert, et al.
Publicado: (2013) -
PEAK1 Y635 phosphorylation regulates cell migration through association with Tensin3 and integrins
por: Zuidema, Alba, et al.
Publicado: (2022) -
Phosphorylation of threonine 1736 in the C-terminal tail of integrin β4 contributes to hemidesmosome disassembly
por: Frijns, Evelyne, et al.
Publicado: (2012)