Regulation of translation initiation by FRAP/mTOR

Article Abstract:

Translation initiation and its regulation by FRAP/mTOR is discussed in this review article. The recruitment process is rate-limiting for translation in many circumstances. Exquisite regulation governs the recruitment. It appears that FRAP/mTOR acts as a nutrient-sensor checkpoint control protein. Rapamycin pharmaceutical use and use of other potential inhibitors will be of interest in ongoing research. Topics in article include rapamycin target proteins, rapamycin effects on translation rates in yeast and in mammalian cells, modular structure of the Tors and FRAP/mTOR, FRAP/mTOR kinase activity and a putative signaling mechanism, dysregulation of PI3K and FRAP/mTOR signaling pathways in cell transformation and cancer, regulation of cell growth and proliferation by PI3K and TOR signaling, and the phsophoinositide-3 kinase pathway signal

Statistical Data Included, Cytochemistry

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Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism

Article Abstract:

Regulation of 4E-BP1 phosphorylation involves a novel two-step mechanism. Results of an investigation show that the phosphorylation of 4E-BP1 by a FRAP/mTOR immunoprecipitate and a baculovirus-expressed FRAP/mTOR protein takes place on two sites only, Trh-46 and Trh-37. A recombinant FRAP/mTOR protein and a FRAP/mTOR immunoprecipitate were used for in vitro kinase assays to phosphorylate 4E-BP1. Phosphopeptide mapping of the in vitro-labeled protein found two 4E-BP1 phosphopeptides that migrated together with phosphophopeptides produced in vivo.

Genetic disorders

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Hierarchical phosphorylation of the translation inhibitor 4E-BP1

Article Abstract:

The in vivo phosphorylation of the translational inhibitor, 4E-BP1, occurs through phosphorylaton of threonine 37/46 followed by threonine 70 and serine 65. Data indicate that phosphorylation of serine 65 and threonine 70 is insufficient to block binding of the inhibitor to the translation factor eIF4E.

Poland, Binding sites (Biochemistry), Active sites (Biochemistry), Amino acids, Amino acid structure-activity relationships

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