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Phosphoregulation of the human SMN complex.

Alma Husedzinovic1, Felix Oppermann2, Stefanie Draeger-Meurer1

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Summary

Phosphorylation regulates the survival motor neuron (SMN) complex localization. This study reveals how serine/threonine and tyrosine phosphorylation control SMN complex accumulation in Cajal bodies (CB).

Keywords:
Functional regulationPhosphorylationProteomicsSMASMN

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The survival motor neuron (SMN) complex is crucial for RNA metabolism, including spliceosomal small nuclear ribonucleoprotein (snRNP) assembly.
  • SMN complex localization within the nucleus, particularly in Cajal Bodies (CB), suggests roles in transcription and splicing.
  • Extensive phosphorylation of the SMN complex indicates a significant role for post-translational modifications in its regulation.

Purpose of the Study:

  • To conduct the first comprehensive phosphoproteome analysis of the intact human SMN complex.
  • To investigate the functional and localization impacts of serine/threonine phosphorylation on SMN complex regulation.
  • To explore the role of tyrosine phosphorylation in SMN complex localization and nuclear accumulation.

Main Methods:

  • Comprehensive phosphoproteome analysis of the intact human SMN complex.
  • Generation of non-phosphorylatable and phosphomimetic SMN variants.
  • Assessment of SMN variants' assembly, snRNP assembly function, and Cajal Body targeting.

Main Results:

  • Identified 48 serine/threonine phosphosites in the SMN complex; 7 of 9 components are phosphoproteins.
  • 12 of 29 identified phosphorylation sites are on SMN itself.
  • Phosphomimetic and non-phosphorylatable SMN variants assemble into complexes and partially rescue snRNP assembly but exhibit impaired Cajal Body targeting.
  • A mutant SMN unable to be phosphorylated on tyrosine residues shows altered localization and nuclear accumulation, indicating tyrosine phosphorylation's regulatory role.

Conclusions:

  • Phosphorylation of serine/threonine and tyrosine residues acts as complex regulatory cues for the SMN complex.
  • These post-translational modifications critically control the subcellular localization and Cajal Body accumulation of the SMN complex.