The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Mechanism of interferon action: Phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated kinase processing site specificity similar to hemin-regulated rabbit reticulocyte kinase
Open accessAbstract
The phosphorylation of purified protein synthesis factors catalyzed by protein kinase preparations isolated from interferon-treated human amnion cells was examined. Ribosomal salt-wash fractions prepared from interferon-treated human cells contained a protein kinase that catalyzed the [γ- 32 P]ATP-mediated phosphorylation of the 38,000-dalton subunit of eukaryotic initiation factor 2 (eIF-2α); this kinase activity was significantly enhanced in interferon-treated as compared to untreated cells. The tryptic [ 32 P]phosphopeptide pattern obtained for eIF-2α phosphorylated by the interferon-mediated human kinase was indistinguishable from the pattern obtained for eIF-2α phosphorylated by the hemin-regulated rabbit reticulocyte kinase when analyzed by thin-layer chromatography with three different solvent systems and by high-voltage electrophoresis. O -[ 32 P]Phosphoserine was liberated by partial acid hydrolysis from eIF-2α phosphorylated by either the human or the rabbit kinase. In addition to the phosphorylation of eIF-2α, interferon treatment of human cells enhanced the phosphorylation of two additional ribosome-associated proteins designated P 1 and P f . The major phosphoester linkage observed for the human, as well as murine, phosphoprotein P 1 was O -phosphoserine. The interferon-mediated phosphorylation of both eIF-2α and protein P 1 was dependent upon the presence of RNA with double-stranded character; P f phosphorylation was not affected by double-stranded RNA. These results suggest that the interferon-mediated ribosome-associated human protein kinase catalyzes the phosphorylation of eIF-2α in a site-specific manner that is apparently identical with the reaction catalyzed by the hemin-regulated rabbit reticulocyte kinase; hence, the phosphorylation of eIF-2 may play a role in regulating the initiation of translation in interferon-treated cells.
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Cites
Greengard, P. (1978) · Science · doi:10.1126/science.22932 · Cited by 965
Phosphorylation of initiation factor eIF-2 and the control of reticulocyte protein synthesis
Farrell, P. J., Balkow, K., Hunt, T., Jackson, R. J., & Trachsel, H. (1977) · Cell · doi:10.1016/0092-8674(77)90330-0 · Cited by 745
Interferon-mediated protein kinase and low-molecular-weight inhibitor of protein synthesis
ROBERTS, W. K., HOVANESSIAN, A., BROWN, R. E., CLEMENS, M. J., & KERR, I. M. (1976) · Nature · doi:10.1038/264477a0 · Cited by 435
Interferon, double-stranded RNA, and protein phosphorylation.
Lebleu, B., Sen, G. C., Shaila, S., Cabrer, B., & Lengyel, P. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.9.3107 · Cited by 319
Interferon action may be mediated by activation of a nuclease by pppA2′p5′A2′p5′A
BAGLIONI, C., MINKS, M. A., & MARONEY, P. A. (1978) · Nature · doi:10.1038/273684a0 · Cited by 307
Taborsky, G. (1974) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60230-2 · Cited by 214
Concerning the mechanism of action of interferon.
Joklik, W. K., & Merigan, T. C. (1966) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.56.2.558 · Cited by 205
Levin, D., & London, I. M. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.3.1121 · Cited by 205
Double-Stranded Poliovirus RNA Inhibits Initiation of Protein Synthesis by Reticulocyte Lysates
Ehrenfeld, E., & Hunt, T. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.5.1075 · Cited by 202
Kramer, G., Cimadevilla, J. M., & Hardesty, B. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.9.3078 · Cited by 201
Cited by
Antiviral Actions of Interferons
Samuel, C. E. (2001) · Clinical Microbiology Reviews · doi:10.1128/cmr.14.4.778-809.2001 · Cited by 2,743
Self-citationMeurs, E., Chong, K., Galabru, J., Thomas, N. S. B., Kerr, I. M., Williams, B. R. G., & Hovanessian, A. G. (1990) · Cell · doi:10.1016/0092-8674(90)90374-n · Cited by 1,017
Interferon-Induced Proteins and the Antiviral State
Staeheli, P. (1990) · Advances in Virus Research · doi:10.1016/s0065-3527(08)60862-3 · Cited by 347
Antisense RNA: Function and Fate of Duplex RNA in Cells of Higher Eukaryotes
Kumar, M., & Carmichael, G. G. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.4.1415-1434.1998 · Cited by 320
The Regulation of Initiation of Mammalian Protein Synthesis
Jagus, R., Anderson, W. F., & Safer, B. (1981) · Progress in Nucleic Acid Research and Molecular Biology · doi:10.1016/s0079-6603(08)60484-5 · Cited by 252
Metadata
- Authors
- Samuel, C. E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1979-02
- Volume
- 76
- Issue
- 2
- Pages
- 600-604
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2091315522
- Cited by
- 262
- References
- 13
- FWCI
- 10.26
- Type
- journal article
- Language
- en
- Open access
- green
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- Samuel, C. E. (1979). Mechanism of interferon action: Phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated kinase processing site specificity similar to hemin-regulated rabbit reticulocyte kinase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.76.2.600
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