Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function. / Pause, A.; Belsham, G.J.; Gingras, A.-C.; Donze, O.; Lin, T.-A.; Lawrence Jr, J.C.; Sonenberg, N.

In: Nature, Vol. 371, 1994, p. 762–767.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Pause, A, Belsham, GJ, Gingras, A-C, Donze, O, Lin, T-A, Lawrence Jr, JC & Sonenberg, N 1994, 'Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function', Nature, vol. 371, pp. 762–767. https://doi.org/10.1038/371762a0

APA

Pause, A., Belsham, G. J., Gingras, A-C., Donze, O., Lin, T-A., Lawrence Jr, J. C., & Sonenberg, N. (1994). Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function. Nature, 371, 762–767. https://doi.org/10.1038/371762a0

Vancouver

Pause A, Belsham GJ, Gingras A-C, Donze O, Lin T-A, Lawrence Jr JC et al. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function. Nature. 1994;371:762–767. https://doi.org/10.1038/371762a0

Author

Pause, A. ; Belsham, G.J. ; Gingras, A.-C. ; Donze, O. ; Lin, T.-A. ; Lawrence Jr, J.C. ; Sonenberg, N. / Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function. In: Nature. 1994 ; Vol. 371. pp. 762–767.

Bibtex

@article{7b7ddde5c6e643d4bbd58a6389786b75,
title = "Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function",
abstract = "The cloning is described of two related human complementary DNAs encoding polypeptides that interact specifically with the translation initiation factor elF-4E, which binds to the messenger RNA 5'-cap structure. Interaction of these proteins with elF-4E inhibits translation but treatment of cells with insulin causes one of them to become hyperphosphorylated and dissociate from elF-4E, thereby relieving the translational inhibition. The action of this new regulator of protein synthesis is therefore modulated by insulin, which acts to stimulate the overall rate of translation and promote cell growth.",
author = "A. Pause and G.J. Belsham and A.-C. Gingras and O. Donze and T.-A. Lin and {Lawrence Jr}, J.C. and N. Sonenberg",
year = "1994",
doi = "10.1038/371762a0",
language = "English",
volume = "371",
pages = "762–767",
journal = "Nature",
issn = "0028-0836",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function

AU - Pause, A.

AU - Belsham, G.J.

AU - Gingras, A.-C.

AU - Donze, O.

AU - Lin, T.-A.

AU - Lawrence Jr, J.C.

AU - Sonenberg, N.

PY - 1994

Y1 - 1994

N2 - The cloning is described of two related human complementary DNAs encoding polypeptides that interact specifically with the translation initiation factor elF-4E, which binds to the messenger RNA 5'-cap structure. Interaction of these proteins with elF-4E inhibits translation but treatment of cells with insulin causes one of them to become hyperphosphorylated and dissociate from elF-4E, thereby relieving the translational inhibition. The action of this new regulator of protein synthesis is therefore modulated by insulin, which acts to stimulate the overall rate of translation and promote cell growth.

AB - The cloning is described of two related human complementary DNAs encoding polypeptides that interact specifically with the translation initiation factor elF-4E, which binds to the messenger RNA 5'-cap structure. Interaction of these proteins with elF-4E inhibits translation but treatment of cells with insulin causes one of them to become hyperphosphorylated and dissociate from elF-4E, thereby relieving the translational inhibition. The action of this new regulator of protein synthesis is therefore modulated by insulin, which acts to stimulate the overall rate of translation and promote cell growth.

U2 - 10.1038/371762a0

DO - 10.1038/371762a0

M3 - Journal article

VL - 371

SP - 762

EP - 767

JO - Nature

JF - Nature

SN - 0028-0836

ER -

ID: 298873491