UDP-glucose dehydrogenase activity and optimal downstream cellular function require dynamic reorganization at the dimer-dimer subunit interfaces

Annastasia S. Hyde, Ashley M. Thelen, Joseph J. Barycki, Melanie A. Simpson

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Background: UDP-glucose dehydrogenase (UGDH) mutants were engineered to perturb hexamer:dimer quaternary structure equilibrium. Results: Dimeric species of UGDH have reduced activity in vitro and in supporting hyaluronan production by cultured cells. Conclusion: Only dynamic UGDH hexamers support robust cellular function. Significance: Manipulation of UGDH activity by hexamer stabilization may offer new therapeutic options in cancer and other pathologies.

Original languageEnglish (US)
Pages (from-to)35049-35057
Number of pages9
JournalJournal of Biological Chemistry
Volume288
Issue number49
DOIs
StatePublished - Dec 6 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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