Pub. Date : 2003 May 2
PMID : 12600984
14 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Interaction between Src and a C-terminal proline-rich motif of Akt is required for Akt activation. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 2 | Interaction between Src and a C-terminal proline-rich motif of Akt is required for Akt activation. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 3 | Here, we provide evidence that tyrosine kinase Src is directly associated with Akt through the interaction between its SH3 domain and a conserved proline-rich motif (PXXP) in the C-terminal regulatory region of Akt. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 4 | Here, we provide evidence that tyrosine kinase Src is directly associated with Akt through the interaction between its SH3 domain and a conserved proline-rich motif (PXXP) in the C-terminal regulatory region of Akt. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 5 | Substitution of the proline residues Pro-424 and Pro-427 by alanines results in loss of Akt activity and phosphorylation induced by the epidermal growth factor (EGF), possibly because these mutations disrupt the interaction between Akt and the SH3 domain of Src. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 6 | Substitution of the proline residues Pro-424 and Pro-427 by alanines results in loss of Akt activity and phosphorylation induced by the epidermal growth factor (EGF), possibly because these mutations disrupt the interaction between Akt and the SH3 domain of Src. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 7 | Substitution of the proline residues Pro-424 and Pro-427 by alanines results in loss of Akt activity and phosphorylation induced by the epidermal growth factor (EGF), possibly because these mutations disrupt the interaction between Akt and the SH3 domain of Src. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 8 | Substitution of the proline residues Pro-424 and Pro-427 by alanines results in loss of Akt activity and phosphorylation induced by the epidermal growth factor (EGF), possibly because these mutations disrupt the interaction between Akt and the SH3 domain of Src. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 9 | Substitution of the proline residues Pro-424 and Pro-427 by alanines results in loss of Akt activity and phosphorylation induced by the epidermal growth factor (EGF), possibly because these mutations disrupt the interaction between Akt and the SH3 domain of Src. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 10 | Substitution of the proline residues Pro-424 and Pro-427 by alanines results in loss of Akt activity and phosphorylation induced by the epidermal growth factor (EGF), possibly because these mutations disrupt the interaction between Akt and the SH3 domain of Src. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 11 | We also showed that phosphorylation of Tyr-315 in Akt induced by Src or EGF is dependent on the integrity of this proline-rich motif. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 12 | Furthermore, the Akt mutant lacking this proline motif fails to block the transcription activity of Forkhead in 293 cells and poorly stimulates the proliferation of Madin-Darby canine kidney cells. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 13 | Taken together, our data suggest that the interaction between the SH3 domain of Src family kinases and the proline-rich motif in the C-terminal regulatory region of Akt is required for tyrosine phosphorylation of Akt and its subsequent activation. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |
| 14 | Taken together, our data suggest that the interaction between the SH3 domain of Src family kinases and the proline-rich motif in the C-terminal regulatory region of Akt is required for tyrosine phosphorylation of Akt and its subsequent activation. | Proline | AKT serine/threonine kinase 1 | Homo sapiens |