2003
DOI: 10.1074/jbc.m307949200
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Ser-64 and Ser-111 in PHAS-I Are Dispensable for Insulin-stimulated Dissociation from eIF4E

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Cited by 27 publications
(24 citation statements)
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“…Recently, several reports have shown that p53 is able to induce or activate novel protein phosphatases (Li et al, 2003;Ueda et al, 2003;Yin et al, 2003) but whether any of these act on 4E-BP1 remains to be established. It may be significant that the greatest p53-induced loss of phosphate from 4E-BP1 in vivo appears to involve Ser 64 , since this site can have a large influence on the binding of the protein to eIF4E (Mothe-Satney et al, 2000b;Karim et al, 2001) (although this conclusion has been challenged; Ferguson et al, 2003). 4E-BP1 is phosphorylated in a hierarchical fashion, with Ser 64 being the last site to be modified when cells are stimulated by serum (Gingras et al, 1999a(Gingras et al, , 2001a.…”
Section: Discussionmentioning
confidence: 99%
“…Recently, several reports have shown that p53 is able to induce or activate novel protein phosphatases (Li et al, 2003;Ueda et al, 2003;Yin et al, 2003) but whether any of these act on 4E-BP1 remains to be established. It may be significant that the greatest p53-induced loss of phosphate from 4E-BP1 in vivo appears to involve Ser 64 , since this site can have a large influence on the binding of the protein to eIF4E (Mothe-Satney et al, 2000b;Karim et al, 2001) (although this conclusion has been challenged; Ferguson et al, 2003). 4E-BP1 is phosphorylated in a hierarchical fashion, with Ser 64 being the last site to be modified when cells are stimulated by serum (Gingras et al, 1999a(Gingras et al, , 2001a.…”
Section: Discussionmentioning
confidence: 99%
“…In HEK 293 cells, for example, their phosphorylation is dependent upon the C-terminal TOS motif . Although there are data that suggest that phosphorylation of this site is required for release of eIF4E from 4E-BP1, the role of phosphorylation of Ser65 is still controversial (Ferguson et al, 2003). Molecular dynamics findings (Tomoo et al, 2005) and earlier biophysical data suggest that phosphorylation of Ser65 and Thr70 is insufficient to bring about release from eIF4E.…”
Section: Control Of the 4e-bps By Mtormentioning
confidence: 99%
“…Akt and mTOR-dependent phosphorylation of Thr37,46 may be the priming event ( Figure 5) (42) that leads to phosphorylation of Thr70 and Ser65; phosphorylation at these four sites may be enough to release eIF4E (70). Some suggest that phosphorylation at Ser65 and Ser111 may not be needed for release of eIF4E (71). Other kinases, such as cdc 2 and ataxia telangiectasia mutated, may act as kinases for 4E-BP1 (72,73).…”
Section: Signaling Regulation Of Mrna Translationmentioning
confidence: 99%