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Triggering Cell Stress and Death Using Conventional UV Laser Confocal Microscopy
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Cellular stress triggers TEL nuclear export via two genetically separable pathways.

Caroline A Hanson1, Lauren D Wood, Scott W Hiebert

  • 1Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA.

Journal of Cellular Biochemistry
|November 21, 2007
PubMed
Summary
This summary is machine-generated.

Cellular stress causes the transcription repressor TEL (translocation ets leukemia, also known as ETV6) to move to the cytoplasm. This relocation is regulated by both SUMOylation and p38-mediated phosphorylation.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Cancer Research

Background:

  • TEL (translocation ets leukemia, also known as ETV6) is a transcription repressor frequently disrupted in pediatric acute lymphocytic leukemia.
  • TEL undergoes post-translational modifications, including SUMOylation at Lys 99, which is crucial for its nuclear export.
  • p38 kinase, activated by cellular stress, phosphorylates TEL, affecting its transcriptional repression activity.

Purpose of the Study:

  • To elucidate the mechanistic basis of how cellular stress impacts TEL's transcriptional repression.
  • To investigate the role of TEL's post-translational modifications in its response to cellular stress.
  • To identify the specific pathways involved in TEL's re-localization under stress conditions.

Main Methods:

  • Induction of cellular stress using osmotic shock and high salt concentrations.
  • Analysis of TEL re-localization using cellular imaging techniques.
  • Investigating the roles of SUMOylation at Lys 99 and phosphorylation at Ser 257 in TEL nuclear export.

Main Results:

  • Osmotic stress induces re-localization of TEL to the cytoplasm, sufficient to be mediated by p38-dependent phosphorylation.
  • Impairment of both Lys 99 SUMOylation and Ser 257 phosphorylation is necessary to inhibit TEL re-localization under high salt stress.
  • Two distinct nuclear export pathways for TEL were identified, regulated by SUMOylation and phosphorylation.

Conclusions:

  • Alteration of TEL cellular localization is an integral part of the cellular stress response.
  • Re-localization of TEL to the cytoplasm is a key regulatory step in controlling TEL function.
  • Understanding TEL's stress response pathways may offer insights into pediatric acute lymphocytic leukemia.