The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
The Rapamycin-sensitive Phosphoproteome Reveals That TOR Controls Protein Kinase A Toward Some But Not All Substrates
Open accessAbstract
Regulation of cell growth requires extensive coordination of several processes including transcription, ribosome biogenesis, translation, nutrient metabolism, and autophagy. In yeast, the protein kinases Target of Rapamycin (TOR) and protein kinase A (PKA) regulate these processes and are thereby the main activators of cell growth in response to nutrients. How TOR, PKA, and their corresponding signaling pathways are coordinated to control the same cellular processes is not understood. Quantitative analysis of the rapamycin-sensitive phosphoproteome combined with targeted analysis of PKA substrates suggests that TOR complex 1 (TORC1) activates PKA but only toward a subset of substrates. Furthermore, we show that TORC1 signaling impinges on BCY1, the negative regulatory subunit of PKA. Inhibition of TORC1 with rapamycin leads to BCY1 phosphorylation on several sites including T129. Phosphorylation of BCY1 T129 results in BCY1 activation and inhibition of PKA. TORC1 inhibits BCY1 T129 phosphorylation by phosphorylating and activating the S6K homolog SCH9 that in turn inhibits the MAP kinase MPK1. MPK1 phosphorylates BCY1 T129 directly. Thus, TORC1 activates PKA toward some substrates by preventing MPK1-mediated activation of BCY1.
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Cites
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855
Perkins, D. N., Pappin, D. J. C., Creasy, D. M., & Cottrell, J. S. (1999) · Electrophoresis · doi:10.1002/(sici)1522-2683(19991201)20:18<3551::aid-elps3551>3.0.co;2-2 · Cited by 8,203
TOR signaling in growth and metabolism
Wullschleger, S., Loewith, R., & Hall, M. N. (2006) · Cell · doi:10.1016/j.cell.2006.01.016 · Cited by 5,787
Self-citationOng, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
New heterologous modules for classical or PCR‐based gene disruptions in Saccharomyces cerevisiae
Wach, A., Brachat, A., Pöhlmann, R., & Philippsen, P. (1994) · Yeast · doi:10.1002/yea.320101310 · Cited by 2,531
Guide to Yeast Genetics and Molecular Biology
Kurtzman, C. P., Guthrie, C., & Fink, G. R. (1993) · Mycologia · doi:10.2307/3760517 · Cited by 2,363
Purification and Characterization
(2006) · Biomacromolecules · doi:10.1002/0470080124.ch3 · Cited by 2,309
Loewith, R., Jacinto, E., Wullschleger, S., Lorberg, A., Crespo, J. L., Bonenfant, D., Oppliger, W., Jenoe, P., & Hall, M. N. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00636-6 · Cited by 1,886
Self-citationOlsen, J. V., de Godoy, L. M. F., Li, G., Macek, B., Mortensen, P., Pesch, R., Makarov, A., Lange, O., Horning, S., & Mann, M. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500030-mcp200 · Cited by 1,510
Cited by
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Benjamin, D., Colombi, M., Moroni, C., & Hall, M. N. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3531 · Cited by 989
Self-citationTarget of Rapamycin (TOR) in Nutrient Signaling and Growth Control
Loewith, R., & Hall, M. N. (2011) · Genetics · doi:10.1534/genetics.111.133363 · Cited by 910
Self-citationThe regulation of autophagy – unanswered questions
Chen, Y., & Klionsky, D. J. (2011) · Journal of Cell Science · doi:10.1242/jcs.064576 · Cited by 591
Quantitative Phosphoproteomics Reveal mTORC1 Activates de Novo Pyrimidine Synthesis
Robitaille, A. M., Christen, S., Shimobayashi, M., Cornu, M., Fava, L. L., Moes, S., Prescianotto-Baschong, C., Sauer, U., Jenoe, P., & Hall, M. N. (2013) · Science · doi:10.1126/science.1228771 · Cited by 525
Self-citationNoda, N. N., & Inagaki, F. (2015) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-060414-034248 · Cited by 356
Metadata
- Authors
- Soulard, A., Cremonesi, A., Moes, S., Schütz, F., Jenö, P., & Hall, M. N.
- Venue
- Molecular Biology of the Cell
- Published
- 2010-10
- Volume
- 21
- Issue
- 19
- Pages
- 3475-3486
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2125025556
- Cited by
- 262
- References
- 73
- FWCI
- 5.91
- Type
- journal article
- Language
- en
- Open access
- green
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