What question did this study set out to answer?

To identify which Ets transcription factors serve as direct nuclear targets of oncogenic Ras signaling and determine the mechanism responsible for their activation.

February 1, 1996Molecular and Cellular BiologyOpen Access

Ras-Mediated Phosphorylation of a Conserved Threonine Residue Enhances the Transactivation Activities of c-Ets1 and c-Ets2

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Authors

BYBeom-Seok YangSanford Burnham Prebys Medical Discovery Institute CHCraig A. HauserGraz University of Technology GHGregory W. HenkelSanford Burnham Prebys Medical Discovery Institute

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Implication

In vitro study reveals that Ras-mediated threonine phosphorylation superactivates Ets1 and Ets2 in mammalian cells, indicating direct nuclear targeting by oncogenic Ras pathways.

Key Points

To identify which Ets transcription factors serve as direct nuclear targets of oncogenic Ras signaling and determine the mechanism responsible for their activation.
Conducted transient transfection reporter assays with Ras-responsive enhancers (Ets-AP-1 and Ets-Ets binding motifs) in NIH 3T3 fibroblasts and RAW264 macrophage-like cells.
Introduced site-directed mutations at conserved amino-terminal threonine residues (Thr38 in Ets1; Thr72 in Ets2) to evaluate functional transactivation.
Performed phosphoamino acid analysis on radiolabeled wild-type and mutant Ets2 proteins in the presence or absence of oncogenic Ras.
Co-expression of oncogenic Ras with Ets1 or Ets2 superactivated Ets-AP-1 reporters 30-fold in NIH 3T3 fibroblasts and 80-fold in RAW264 cells, whereas other Ets factors showed no activation.
Substitution of the conserved threonine residue with alanine (Thr38Ala in Ets1, Thr72Ala in Ets2) completely abolished Ras-dependent transcriptional superactivation.
Ras signaling stimulated threonine-specific phosphorylation on Ets2, which was absent when Thr72 was mutated to alanine or serine.

Cite This Study

Yang et al. (1996) studied this question.

synapsesocial.com/papers/6a76a628bf7962ca510614b7 https://doi.org/10.1128/mcb.16.2.538

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Implication

In vitro study reveals that Ras-mediated threonine phosphorylation superactivates Ets1 and Ets2 in mammalian cells, indicating direct nuclear targeting by oncogenic Ras pathways.

Ras-Mediated Phosphorylation of a Conserved Threonine Residue Enhances the Transactivation Activities of c-Ets1 and c-Ets2

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Implication

Key Points

Cite This Study

Ras-Mediated Phosphorylation of a Conserved Threonine Residue Enhances the Transactivation Activities of c-Ets1 and c-Ets2

Discussion

Member takes

Implication

Key Points

Cite This Study

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