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Derepression by depolymerization; structural insights into the regulation of Yan by Mae.

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The protein Mae depolymerizes Yan, a transcriptional repressor, through its SAM domain. This novel mechanism allows Mae to regulate Yan activity, impacting receptor tyrosine kinase signaling.

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Area of Science:

  • Molecular Biology
  • Transcriptional Regulation
  • Protein-Protein Interactions

Background:

  • Yan is an ETS family transcriptional repressor.
  • Yan activity is regulated by receptor tyrosine kinase (RTK) signaling through the Ras/MAPK pathway.
  • Mae protein facilitates Yan phosphorylation and downregulation.

Purpose of the Study:

  • To investigate the interaction between Yan and Mae.
  • To elucidate the mechanism by which Mae regulates Yan.
  • To understand the role of SAM domains in Yan-Mae interaction and transcriptional control.

Main Methods:

  • Co-immunoprecipitation to study Yan-Mae interaction.
  • SAM domain analysis.
  • Crystal structure determination of Yan-SAM/Mae-SAM complex.
  • In vivo functional assays with Mae mutations.

Main Results:

  • Yan and Mae interact via their SAM domains.
  • Yan repression requires Yan-SAM polymerization into higher-order structures.
  • Mae-SAM specifically binds to a polymerization-critical surface on Yan-SAM.
  • Mae-SAM has a 1000-fold higher affinity for Yan-SAM than Yan-SAM self-binding and can depolymerize Yan-SAM.
  • Mutations disrupting Mae's SAM domain interaction abolish Mae's derepression function in vivo.

Conclusions:

  • Mae depolymerizes Yan-SAM polymers, representing a novel transcriptional control mechanism.
  • Mae-mediated depolymerization sensitizes Yan for RTK signaling regulation.
  • The Yan-SAM/Mae-SAM interaction provides insights into SAM domain-mediated protein assembly and regulation.