mTORC1-Mediated Cell Proliferation, But Not Cell Growth, Controlled by the 4E-BPs

Author:

Dowling Ryan J. O.1,Topisirovic Ivan1,Alain Tommy1,Bidinosti Michael1,Fonseca Bruno D.1,Petroulakis Emmanuel1,Wang Xiaoshan1,Larsson Ola1,Selvaraj Anand2,Liu Yi3,Kozma Sara C.2,Thomas George2,Sonenberg Nahum1

Affiliation:

1. Department of Biochemistry and Goodman Cancer Research Centre, McGill University, Montreal, Quebec H3A 1A3, Canada.

2. Department of Cancer and Cell Biology, Metabolic Diseases Institute, University of Cincinnati, Cincinnati, OH 45237, USA.

3. Intellikine, La Jolla, CA 92037, USA.

Abstract

Proliferation Control The protein complex mTORC1, which contains the protein kinase known as mammalian target of rapamycin, is an important regulator of cell proliferation and cell size. Among many targets, mTORC1 phosphorylates the eukaryotic translation initiation factor eIF4E–binding proteins (4E-BPs), thus controlling translation of proteins that regulate proliferation. Dowling et al. (p. 1172 ) used mice lacking expression of the 4E-BPs to show that these proteins contribute to mTORC1's activation of cell proliferation, but are dispensable for the effects of mTORC1 on cell growth. The latter required another mTORC1 target—the ribosomal protein S6 kinase. mTORC1 inhibitors are being explored as potential anticancer agents, and the presence of 4E-BPs was necessary for mTORC1 inhibitors to reduce the number and size of colonies formed by transformed mouse cells.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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