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Updated: Jun 12, 2026

SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
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SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

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Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and

A F Yousef1, G J Fonseca, P Pelka

  • 1Department of Microbiology and Immunology, The University of Western Ontario, London, Ontario, Canada.

Oncogene
|June 15, 2010
PubMed

Insights

Adenovirus E1A oncogene protein binds UBC9, interfering with polySUMOylation. This interaction regulates cell reprogramming and yeast pseudohyphal growth, revealing a novel viral mechanism.

Area of Science:

  • Cellular biology
  • Virology
  • Molecular mechanisms

Background:

  • Hub proteins are central regulators of cellular processes.
  • Viral oncogenes, like adenovirus E1A, can reprogram cells by targeting cellular hubs.
  • Short linear motifs/molecular recognition features (MoRFs) mediate interactions between viral oncogenes and cellular proteins.

Purpose of the Study:

  • To identify novel functional regions (MoRFs) within the adenovirus E1A oncoprotein.
  • To investigate the interaction between E1A and the SUMO conjugase UBC9.
  • To elucidate the role of polySUMOylation in E1A-mediated cellular processes.

Main Methods:

  • Screening of E1A portions for activation of yeast pseudohyphal growth.
  • Identification of a novel MoRF (EVIDLT) in E1A conserved region 2.
  • Assessing the binding of E1A MoRF to UBC9 and its effect on SUMOylation.

Main Results:

  • A novel E1A MoRF (EVIDLT) was identified, binding to UBC9.
  • E1A interaction with UBC9 interferes with polySUMOylation, not monoSUMOylation.
  • PolySUMOylation was shown to regulate E1A-mediated pseudohyphal growth and PML body reorganization.

Conclusions:

  • The E1A oncogene interacts with UBC9 via a novel MoRF, mimicking normal SUMO-UBC9 binding.
  • This interaction provides a mechanism for viral modulation of cellular polySUMOylation.
  • E1A's interference with polySUMOylation impacts cellular processes regulated by this modification.

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