Title : Phosphorylation of threonine residues on Shc promotes ligand binding and mediates crosstalk between MAPK and Akt pathways in breast cancer cells.

Pub. Date : 2018 Jan

PMID : 29208567






3 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Phosphorylation of threonine residues on Shc promotes ligand binding and mediates crosstalk between MAPK and Akt pathways in breast cancer cells. Threonine mitogen-activated protein kinase 1 Homo sapiens
2 To explore how Erk-mediated threonine phosphorylation on Shc might play a role in the dysregulation of signalling events, we investigated how Shc affects pathways downstream of EGF receptor. Threonine mitogen-activated protein kinase 1 Homo sapiens
3 Using an in vitro model and biophysical analysis, we show that Shc threonine phosphorylation is responsible for elevated Akt and Erk signalling, potentially through the recruitment of the 14-3-3 zeta and Pin-1 proteins. Threonine mitogen-activated protein kinase 1 Homo sapiens