Overview: phosphorylation and translation control - PubMed (original) (raw)
Review
Overview: phosphorylation and translation control
J W Hershey. Enzyme. 1990.
Abstract
Protein synthesis is controlled by the phosphorylation of proteins comprising the translational apparatus. At least 12 initiation factor polypeptides, 3 elongation factors and a ribosomal protein are implicated. Stimulation of translation correlates with enhanced phosphorylation of eIF-4F, eIF-4B, eIF-2B, eIF-3 and ribosomal protein S6, whereas inhibition correlates with phosphorylation of eEF-2 and the alpha-subunit of eIF-2. Strong evidence for regulatory roles exists for eIF-2, eIF-4F and eEF-2, whereas changes in other factor activities due to phosphorylation remain to be demonstrated. Regulation of the specific activity of the translational apparatus by phosphorylation appears to be a general mechanism for the control of rates of global protein synthesis, and may also play a role in modulating the translation of specific mRNAs.
Similar articles
- Protein phosphorylation in translational control.
Proud CG. Proud CG. Curr Top Cell Regul. 1992;32:243-369. doi: 10.1016/b978-0-12-152832-4.50008-2. Curr Top Cell Regul. 1992. PMID: 1318183 Review. No abstract available. - Signal transduction and regulation of translation initiation.
Frederickson RM, Sonenberg N. Frederickson RM, et al. Semin Cell Biol. 1992 Apr;3(2):107-15. doi: 10.1016/s1043-4682(10)80020-0. Semin Cell Biol. 1992. PMID: 1611042 Review.
Cited by
- A new yeast translation initiation factor suppresses a mutation in the eIF-4A RNA helicase.
Coppolecchia R, Buser P, Stotz A, Linder P. Coppolecchia R, et al. EMBO J. 1993 Oct;12(10):4005-11. doi: 10.1002/j.1460-2075.1993.tb06078.x. EMBO J. 1993. PMID: 8404866 Free PMC article. - The plant translational apparatus.
Browning KS. Browning KS. Plant Mol Biol. 1996 Oct;32(1-2):107-44. doi: 10.1007/BF00039380. Plant Mol Biol. 1996. PMID: 8980477 Review. - The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR.
Donzé O, Abbas-Terki T, Picard D. Donzé O, et al. EMBO J. 2001 Jul 16;20(14):3771-80. doi: 10.1093/emboj/20.14.3771. EMBO J. 2001. PMID: 11447118 Free PMC article. - The metabolic basis of whole-organism RNA and phosphorus content.
Gillooly JF, Allen AP, Brown JH, Elser JJ, Martinez del Rio C, Savage VM, West GB, Woodruff WH, Woods HA. Gillooly JF, et al. Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11923-7. doi: 10.1073/pnas.0504756102. Epub 2005 Aug 9. Proc Natl Acad Sci U S A. 2005. PMID: 16091465 Free PMC article. - Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster.
Haile DJ, Rouault TA, Tang CK, Chin J, Harford JB, Klausner RD. Haile DJ, et al. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7536-40. doi: 10.1073/pnas.89.16.7536. Proc Natl Acad Sci U S A. 1992. PMID: 1502165 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Miscellaneous