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Updated: Aug 7, 2026

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

14-3-3tau associates with a translational control factor FKBP12-rapamycin-associated protein in T-cells after

H Mori1, M Inoue, M Yano

  • 1Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima, Japan.

FEBS Letters
|February 9, 2000
PubMed

Insights

The 14-3-3 protein family regulates cell signaling and the cell cycle. Pervanadate treatment induced 14-3-3tau to associate with FKBP12-rapamycin-associated protein (FRAP), promoting FRAP autophosphorylation.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Proteins of the 14-3-3 family are crucial regulators of signaling pathways and the cell cycle.
  • They interact with and modulate various proteins, including protooncogenes, oncogenes, Cdc25 phosphatases, and phosphatidylinositol 3-kinase.

Purpose of the Study:

  • To investigate the interaction between 14-3-3tau and the translational control factor FKBP12-rapamycin-associated protein (FRAP).
  • To determine the effect of protein tyrosine phosphatase inhibition on this interaction and FRAP activity.

Main Methods:

  • Jurkat T-cells were treated with pervanadate, a protein tyrosine phosphatase inhibitor.
  • Coimmunoprecipitation assays were performed using various FRAP mutants coexpressed with 14-3-3tau in COS-7 cells.

Main Results:

  • Pervanadate treatment induced the association of 14-3-3tau with FRAP in Jurkat T-cells.
  • This association was accompanied by significant autophosphorylation of FRAP.
  • Mapping studies revealed that 14-3-3tau binds to the C-terminal region of FRAP at a site distinct from previously predicted binding motifs.

Conclusions:

  • 14-3-3tau interacts with FRAP, a translational control factor, in response to protein tyrosine phosphatase inhibition.
  • The interaction site is located in the C-terminal domain of FRAP and is not a canonical 14-3-3 binding motif.
  • This finding sheds light on novel regulatory mechanisms involving 14-3-3 proteins in cellular signaling and translational control.

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