The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins.
Open accessAbstract
The immunosuppressant rapamycin (RAP) has been demonstrated to specifically inhibit the activity of p70 S6 kinase (p70s6k) and subsequent phosphorylation of ribosomal S6 protein in mammalian cells. Addition of RAP to proliferating lymphoid cells resulted in inhibition of protein synthesis before any changes in the rate of cell proliferation. When the cellular composition of proteins was examined by gel electrophoresis, RAP dramatically inhibited synthesis of selective proteins, particularly elongation factor 2 (eEF-2). The inhibition of eEF-2 synthesis by RAP was at the translational level. Further, RAP inhibited the polysomal association of mRNAs encoding not only eEF-2 but also elongation factor 1-alpha and ribosomal proteins without affecting mRNA translation of any of a number of nonribosomal proteins. Since levels of activity of p70s6k are correlated with the rate of biosynthesis of eEF-2, p70s6k might be involved in coordinate translational regulation of ribosomal protein mRNAs in higher eukaryotes, which have a conserved sequence at their 5' end. Specific inhibition of ribosomal protein synthesis likely explains the differential antiproliferative effect of RAP on proliferating and mitogen-activated quiescent cells.
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Cites
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Human cyclin A is adenovirus E1A-associated protein p60 and behaves differently from cyclin B
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Rapamycin-Induced Inhibition of the 70-Kilodalton S6 Protein Kinase
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Rapamycin selectively inhibits interleukin-2 activation of p70 S6 kinase
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p70s6k function is essential for G1 progression
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Self-citationMAP2 kinase and 70K S6 kinase lie on distinct signalling pathways
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Cited by
Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
Regulation of translation initiation by FRAP/mTOR
Gingras, A.-C., Raught, B., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.887201 · Cited by 1,545
Hara, K., Yonezawa, K., Weng, Q.-P., Kozlowski, M. T., Belham, C., & Avruch, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14484 · Cited by 1,367
The tor pathway: a target for cancer therapy
Bjornsti, M.-A., & Houghton, P. J. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1362 · Cited by 1,314
Fingar, D. C., & Blenis, J. (2004) · Oncogene · doi:10.1038/sj.onc.1207542 · Cited by 1,247
Metadata
- Authors
- Terada, N., Patel, H. R., Takase, K., Kohno, K., Nairn, A. C., & Gelfand, E. W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1994-11-22
- Volume
- 91
- Issue
- 24
- Pages
- 11477-11481
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2048794678
- Cited by
- 353
- References
- 27
- FWCI
- 7.11
- Type
- journal article
- Language
- en
- Open access
- green
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- Terada, N., Patel, H. R., Takase, K., Kohno, K., Nairn, A. C., & Gelfand, E. W. (1994). Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.91.24.11477
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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