Mutation of the salt bridge-forming residues in the ETV6-SAM domain interface blocks ETV6-NTRK3-induced cellular transformation

Naniye Cetinbas, Helen Huang-Hobbs, Cristina Tognon, Gabriel Leprivier, Jianghong An, Steven McKinney, Mary Bowden, Connie Chow, Martin Gleave, Lawrence P. McIntosh, Poul H. Sorensen

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Background: SAM domain-mediated polymerization is essential for ETV6-NTRK3 (EN)-induced cellular transformation. Results: Mutation of a salt bridge at the SAM polymer interface weakens SAM polymerization and abrogates EN transformation. Conclusion: Intermolecular electrostatic interactions are important for SAM domain polymerization and EN transformation. Significance: These studies provide further insights into the mechanisms by which ETV6-SAM domain mediates EN transformation.

Original languageEnglish (US)
Pages (from-to)27940-27950
Number of pages11
JournalJournal of Biological Chemistry
Volume288
Issue number39
DOIs
StatePublished - Sep 27 2013
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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