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The mRNA-Binding Protein HuR Is a Kinetically-Privileged Electrophile Sensor.

Jesse R Poganik1,2, Alexandra K Van Hall-Beauvais1, Marcus J C Long2

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Summary
This summary is machine-generated.

The RNA-binding protein HuR, but not AUF1, acts as a specific sensor for the electrophilic lipid 4-hydroxynonenal (HNE). HuR depletion alters cell viability and the antioxidant response, highlighting its complex regulatory role.

Keywords:
4-hydroxynonenalAUF1HuRNrf2antioxidant responseelectrophile sensormRNAmRNA-binding proteinsensors

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Area of Science:

  • Cellular stress response
  • Oxidative stress signaling
  • mRNA regulation

Background:

  • HuR and AUF1 are critical mammalian stress sensors.
  • Electrophilic lipids like prostaglandin A2 and redox signals influence these proteins.
  • 4-hydroxynonenal (HNE) is a key redox-linked lipid-derived electrophile.

Purpose of the Study:

  • To investigate the sensing capabilities of HuR and AUF1 towards HNE.
  • To elucidate the specific mechanisms and cellular consequences of HNE sensing by HuR.
  • To understand HuR's role in regulating the Nrf2-driven antioxidant response.

Main Methods:

  • Utilized the T-REX electrophile delivery platform for precise HNE application.
  • Employed HEK293T cells for in vitro studies.
  • Conducted mutagenesis studies targeting specific cysteine residues in HuR (C13).
  • Performed cell depletion experiments for HuR and assessed cell viability and antioxidant response.

Main Results:

  • HuR, not AUF1, is a kinetically privileged sensor of HNE in HEK293T cells.
  • HNE sensing by HuR is mediated through a specific cysteine residue, C13.
  • HuR depletion leads to significant changes in cell viability and Nrf2-transcription-factor-driven antioxidant response.
  • Mutagenesis of C13 alone did not fully explain HuR's stress responsivity.

Conclusions:

  • HuR is a specific sensor for the electrophilic lipid HNE, functioning via C13.
  • HuR plays a crucial role in modulating cell viability and antioxidant responses to HNE.
  • The regulation of the Nrf2/antioxidant response by HuR is complex and context-dependent, extending beyond simple C13-mediated sensing.