Cargando…
A p130(Cas) tyrosine phosphorylated substrate domain decoy disrupts v-Crk signaling
BACKGROUND: The adaptor protein p130(Cas) (Cas) has been shown to be involved in different cellular processes including cell adhesion, migration and transformation. This protein has a substrate domain with up to 15 tyrosines that are potential kinase substrates, able to serve as docking sites for pr...
Autores principales: | Kirsch, Kathrin H, Kensinger, Margaret, Hanafusa, Hidesaburo, August, Avery |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2002
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC117778/ https://www.ncbi.nlm.nih.gov/pubmed/12119061 http://dx.doi.org/10.1186/1471-2121-3-18 |
Ejemplares similares
-
Iterative Tyrosine Phosphorylation Controls Non-canonical Domain Utilization in Crk
por: Sriram, Ganapathy, et al.
Publicado: (2014) -
uPAR promotes formation of the p130Cas–Crk complex to activate Rac through DOCK180
por: Smith, Harvey W., et al.
Publicado: (2008) -
Ibuprofen inhibited migration of skeletal muscle cells in association with downregulation of p130cas and CrkII expressions
por: Liao, Chih-Hao, et al.
Publicado: (2019) -
Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase non-receptor 14
por: Zhang, Peng, et al.
Publicado: (2012) -
Phosphorylation of Tyrosine Residues 31 and 118 on Paxillin Regulates Cell Migration through an Association with Crk in Nbt-II Cells
por: Petit, Valérie, et al.
Publicado: (2000)