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Phosphorylation acts positively and negatively to regulate MRTF-A subcellular localisation and activity

Richard Panayiotou1, Francesc Miralles1, Rafal Pawlowski1

  • 1Signaling and Transcription Group, Francis Crick Institute, London, United Kingdom.

Elife
|June 16, 2016
PubMed

Insights

Myocardin-related transcription factors (MRTF-A) phosphorylation by Rho and ERK signals regulates cytoskeletal gene expression. Phosphorylation controls MRTF-A

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Myocardin-related transcription factors (MRTF-A and MRTF-B) partner with SRF to regulate cytoskeletal genes.
  • MRTF nuclear accumulation is controlled by G-actin levels.
  • The roles of MRTF phosphorylation and nuclear export mechanisms are not well understood.

Purpose of the Study:

  • Investigate the functional significance of MRTF-A phosphorylation.
  • Identify signals and elements governing MRTF-A nuclear export.

Main Methods:

  • Phosphorylation site mapping of MRTF-A.
  • Analysis of Rho- and ERK-dependent signaling pathways.
  • Assessment of MRTF-A nuclear import/export dynamics.

Main Results:

  • Rho-dependent phosphorylation relieves inhibition by nuclear actin.
  • Serum-induced phosphorylation at S/T-P motifs is crucial for transcriptional activation.
  • ERK-mediated S98 phosphorylation promotes nuclear import by inhibiting G-actin binding.
  • S33 phosphorylation enhances Crm1-dependent nuclear export.

Conclusions:

  • MRTF-A phosphorylation has dual roles in regulating its activity.
  • Phosphorylation modulates MRTF-A interactions with actin and nuclear export machinery.
  • This study elucidates a complex regulatory network controlling MRTF-A function.
Keywords:
NESRPELSRFactincell biologychromosomesgeneshumanmousesignal transductiontranscription

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