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Conformational landscape of multidomain SMAD proteins.

Tiago Gomes1, Pau Martin-Malpartida1, Lidia Ruiz1

  • 1Institute for Research in Biomedicine, The Barcelona Institute of Science and Technology, Baldiri Reixac, 10, Barcelona 08028, Spain.

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Summary

SMAD proteins, key to TGFβ signaling, reveal complex structures. Their flexible linkers enable regulation, with SMAD2 forming diverse complexes while SMAD4 remains monomeric.

Keywords:
Intrinsically disordered regionsMulti-domain proteinsSMADTGFβ signalingTranscription factor

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • SMAD transcription factors are central effectors of the transforming growth factor β (TGFβ) signaling pathway.
  • The complex architecture of SMAD proteins, featuring globular domains and flexible linkers, has historically hindered full-length structure determination.

Purpose of the Study:

  • To elucidate the full-length (FL) structures of SMAD4 and SMAD2 proteins.
  • To understand the role of protein flexibility and domain interactions in SMAD protein function and regulation.

Main Methods:

  • Integrative structural biology approach combining Small-angle X-ray scattering (SAXS), Nuclear Magnetic Resonance (NMR) spectroscopy, and X-ray crystallography.
  • Computational modeling was employed to complement experimental data and describe protein ensembles.

Main Results:

  • Both SMAD4FL and SMAD2FL proteins exist as ensembles of conformations, with flexible linkers connecting globular domains.
  • SMAD4FL was found to be monomeric, while SMAD2FL exhibited monomer-dimer-trimer states, regulated by MH2 domain interactions.
  • Linker flexibility was shown to be crucial for DNA and protein binding, modulating overall protein structure.

Conclusions:

  • The inherent flexibility of SMAD proteins represents a novel regulatory mechanism.
  • SMAD2FL dimers, observed independently of activation state and concentration, are proposed as fundamental units for SMAD complex quaternary structures.
  • This study provides critical insights into the structural dynamics and assembly of SMAD proteins in TGFβ signaling.