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PIN1 Provides Dynamic Control of MYC in Response to Extrinsic Signals

Gabriel M Cohn1, Daniel F Liefwalker1, Ellen M Langer1,2

  • 1Department of Molecular and Medical Genetics, School of Medicine, Oregon Health and Science University, Portland, OR, United States.

Frontiers in Cell and Developmental Biology
|April 18, 2020
PubMed

Insights

Peptidyl-prolyl cis/trans isomerase (PIN1) regulates c-MYC stability and function by isomerizing phosphorylated MYC. PIN1 controls MYC

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • PIN1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that modifies phosphorylated proteins.
  • c-MYC (MYC) is a key transcription factor regulated by phosphorylation at Serine 62.
  • PIN1 facilitates conformational changes in phosphorylated MYC, impacting its function.

Purpose of the Study:

  • To describe the molecular mechanisms of PIN1 target recognition.
  • To elucidate PIN1's role in the temporal and spatial regulation of MYC.
  • To explain how PIN1 calibrates cellular responses to stress via MYC nuclear pore localization.

Main Methods:

  • The study is a perspective, synthesizing existing research and data.
  • Focuses on molecular mechanisms of PIN1-MYC interaction.
  • Discusses cellular localization and functional consequences.

Main Results:

  • PIN1 isomerizes phosphorylated MYC at Proline 63, creating distinct MYC pools.
  • PIN1 regulates MYC stability, DNA binding timing, and subnuclear localization.
  • Phosphorylated MYC associates with the nuclear pore basket in a PIN1-dependent manner.

Conclusions:

  • PIN1 is crucial for regulating MYC's molecular timing and cellular localization.
  • PIN1-mediated MYC trafficking at the nuclear pore calibrates cellular responses.
  • Understanding PIN1-MYC interactions offers insights into cellular signaling and stress response.
Keywords:
Pin1c-Mycisomerizationnuclear pore complexphosphorylation

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