Title : Eukaryotic Initiation Factor 4E (eIF4E) sequestration mediates 4E-BP1 response to rapamycin.

Pub. Date : 2019 Mar 15

PMID : 30552925






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Eukaryotic Initiation Factor 4E (eIF4E) sequestration mediates 4E-BP1 response to rapamycin. Sirolimus eukaryotic translation initiation factor 4E binding protein 1 Homo sapiens
2 Based on the well-described effects of mTORC1/rapamycin complex on 4E-BP1 phosphorylation/s, it is generally accepted that rapamycin is a global inhibitor of cap-dependent translation. Sirolimus eukaryotic translation initiation factor 4E binding protein 1 Homo sapiens
3 We have previously shown that 4E-BP1 resistance to rapamycin was overcome by the stoichiometric abundance of S6K1. Sirolimus eukaryotic translation initiation factor 4E binding protein 1 Homo sapiens
4 Now we present evidence that the TOS-bearing amino terminal domain of S6K1 is sufficient to relieve the rapamycin resistance of 4E-BP1 as TOS deleted variants of S6K1, active or inactive with regard to S6K1 activity failed to bring about relief of 4E-BP1 resistance to rapamycin. Sirolimus eukaryotic translation initiation factor 4E binding protein 1 Homo sapiens
5 The data presented in this study identifies eIF4E and not Raptor as a cellular factor responsible to regulate rapamycin sensitivity of 4E-BP1 suggesting that the phosphorylation dynamics and rapamycin sensitivity of 4E-BP1 and S6K1 are regulated independently. Sirolimus eukaryotic translation initiation factor 4E binding protein 1 Homo sapiens