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Interplay between SUMOylation and NEDDylation regulates RPL11 localization and function.

Ahmed El Motiam1, Santiago Vidal1, Carlos F de la Cruz-Herrera2,3

  • 1Centro de Investigación en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidade de Santiago de Compostela e Instituto de Investigaciones Sanitarias, Santiago de Compostela, Spain.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|July 20, 2018
PubMed
Summary

Small ubiquitin-related modifier (SUMO) protein conjugation to ribosomal protein L11 (RPL11) regulates p53 signaling. SUMOylation impacts RPL11 localization and its interplay with neural precursor cell-expressed developmentally downregulated 8 (NEDD8) conjugation.

Keywords:
ARFNEDD8SUMOp53

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Ribosomal protein L11 (RPL11) is a key mediator integrating cellular stress signals into p53 responses.
  • The interplay between post-translational modifications and RPL11 function in stress signaling remains incompletely understood.

Purpose of the Study:

  • To investigate the role of small ubiquitin-related modifier (SUMO)ylation in regulating RPL11 function and its impact on p53 signaling.
  • To elucidate the relationship between SUMOylation and other ubiquitin-like modifications, such as NEDDylation, on RPL11.

Main Methods:

  • Analysis of RPL11 modification by SUMO1 and SUMO2 via covalent conjugation.
  • Assessment of SUMO's effect on neural precursor cell-expressed developmentally downregulated 8 (NEDD8) conjugation to RPL11.
  • Investigation of RPL11 translocation using microscopy and the role of Ubc9 in p53 activation.

Main Results:

  • SUMO1 and SUMO2 covalently modify RPL11.
  • SUMOylation negatively regulates NEDD8 conjugation to RPL11 and promotes its export from nucleoli.
  • SUMOylation of RPL11 is induced by ribosomal stress and alternate reading frame protein upregulation, requiring Ubc9 for p53 activation.

Conclusions:

  • SUMOylation of RPL11 is a novel regulatory mechanism in the p53-mediated stress response.
  • A previously uncharacterized interplay between SUMOylation and NEDDylation governs RPL11 localization and activity.
  • These findings reveal a new layer of control in cellular stress signaling pathways.