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A biosensor for MAPK-dependent Lin28 signaling.

Laurel M Oldach1, Kirill Gorshkov1,2, William T Mills3

  • 1Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205.

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|March 16, 2018
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Summary
This summary is machine-generated.

The RNA-binding protein Lin28a, crucial for growth, is stabilized by TRBP via MAPK signaling. This study visualizes their interaction, revealing phosphorylation

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Lin28a is a key RNA-binding protein regulating cellular growth and pluripotency.
  • Its intracellular levels are tightly controlled, primarily through posttranscriptional mechanisms.
  • Mitogen-activated protein kinase (MAPK) signaling can elevate Lin28a levels in differentiated cells.

Purpose of the Study:

  • To elucidate the molecular and spatiotemporal mechanisms controlling Lin28a levels.
  • To dissect the interaction between Lin28a and the HIV TAR RNA-binding protein (TRBP).
  • To develop biosensors for visualizing and monitoring this interaction in real-time.

Main Methods:

  • Protein truncation analysis to identify interacting domains of Lin28a and TRBP.
  • Site-directed mutagenesis to investigate the role of specific phosphorylation sites (Ser152 in TRBP, Ser200 in Lin28a).
  • Development and application of fluorescence resonance energy transfer (FRET)-based biosensors (bimolecular and unimolecular) in living cells.
  • Coimaging of FRET sensor response with Erk activation.

Main Results:

  • Identified specific truncated domains of Lin28a and TRBP sufficient for coassociation and mutual protein level elevation.
  • Demonstrated the requirement of MAPK-dependent phosphorylation of TRBP (Ser152) and Lin28a (Ser200) for TRBP-mediated Lin28a stabilization.
  • Successfully developed and validated FRET sensors to dynamically monitor Lin28a-TRBP interactions in response to growth factor stimulation in living cells.
  • Correlated FRET sensor activity with Erk activation, providing insights into MAPK signaling pathways.

Conclusions:

  • The interaction between Lin28a and TRBP, regulated by specific phosphorylation events and MAPK signaling, is critical for controlling Lin28a protein levels.
  • Developed FRET biosensors provide a powerful tool for real-time visualization and quantitative analysis of this dynamic protein-protein interaction in cellular contexts.
  • This work deepens the understanding of posttranscriptional regulation of pluripotency factors and cellular growth control mechanisms.