Mutational analysis of sites in the translational regulator, PHAS-I, that are selectively phosphorylated by mTOR

Daqing Yang, Gregory J. Brunn, John C. Lawrence

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Results obtained with PHAS-I proteins having Ser to Ala mutations in the five known phosphorylation sites indicate that mTOR preferentially phosphorylates Thr36 and Thr45. The effects of phosphorylating these sites on eIF4E binding were assessed in a far-Western analysis with a labeled eIF4E probe. Phosphorylation of Thr36 only slightly attenuated binding of PHAS-I to eIF4E, while phosphorylation of Thr45 markedly inhibited binding. Phosphorylation of neither site affected the electrophoretic mobility of the protein, indicating that results of studies that rely solely on a gel-shift assay to assess changes in PHAS-I phosphorylation must be interpreted with caution.

Original languageEnglish (US)
Pages (from-to)387-390
Number of pages4
JournalFEBS Letters
Volume453
Issue number3
DOIs
StatePublished - Jun 25 1999

Keywords

  • 4E-BP1
  • Mitogen-associated protein kinase
  • mRNA translation initiation
  • mTOR

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