regulation of eif-4e and p70s6 kinase
PAG Title | regulation of eif-4e and p70s6 kinase |
PAG ID | WAG001249 |
Type | P |
Source Link | BioCarta |
Publication Reference | NA |
PAG Description | eIF-4F and p70 S6 kise play critical roles in translatiol regulation. eIF-4F is a complex whose functions include the recognition of the mR 5' cap structure (eIF-4E), delivery of an R helicase to the 5' region (eIF-4A), bridging of the mR and the ribosome (eIF-4G), and circularization of the mR via interaction between eIF-4G and the poly(A) binding protein (PABP). Several stimuli, including growth factors and cytokines, regulate the eIF-4 complex and p70 S6 kise by initiating a phosphorylation cascade involving the sequential activation of PI3-K, PDK1/2, Akt/PKB, and FRAP/mTOR kise. FRAP/mTOR, together with an unidentified kise, phosphorylates 4E-BP, leading to its dissociation from and activation of eIF-4E. MNK1/2, activated by ERK and p38 MAPK, phosphorylates and activates eIF-4E. Both processes contribute to the association of eIF-4E and eIF-4G to form the active eIF-4F complex, a necessary component of the 48S initiation complex. Phosphorylation of ribosomal protein S6 by p70 S6 kise stimulates the translation of mRs with a 5' oligopyrimidine tract which typically encode components of the protein synthesis. |
Species | Homo sapiens |
Quality Metric Scores | nCoCo Score: 1,938 |
Information Content | Rich |
Other IDs | |
Base PAG ID | WAG001249 |
Human Phenotyte Annotation | |
Curator | PAGER curation team |
Curator Contact | PAGER-contact@googlegroups.com |
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