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Substrate modification with lysine 63-linked ubiquitin chains through the UBC13-UEV1A ubiquitin-conjugating enzyme.

Protein modification with lysine 63-linked ubiquitin chains has been implicated in the non-proteolytic regulation of signaling pathways. To understand the molecular mechanisms underlying this process, we have developed an in vitro system to examine the activity of the ubiquitin-conjugating enzyme UBC13-UEV1A with TRAF6 in which TRAF6 serves as both a ubiquitin ligase and substrate for modification. Although TRAF6 potently stimulates the activity of UBC13-UEV1A to synthesize ubiquitin chains, it is not appreciably ubiquitinated. We have determined that the presentation of Lys(63) of ubiquitin by UEV1A suppresses TRAF6 modification. Based on our observations, we propose that the modification of proteins with Lys(63)-linked ubiquitin chains occurs through a UEV1A-independent substrate modification and UEV1A-dependent Lys(63)-linked ubiquitin chain synthesis mechanism.

Pubmed ID: 17709375

Authors

  • Petroski MD
  • Zhou X
  • Dong G
  • Daniel-Issakani S
  • Payan DG
  • Huang J

Journal

The Journal of biological chemistry

Publication Data

October 12, 2007

Associated Grants

None

Mesh Terms

  • Animals
  • Escherichia coli
  • Humans
  • Lysine
  • Mice
  • Models, Molecular
  • Protein Binding
  • Substrate Specificity
  • TNF Receptor-Associated Factor 6
  • Transcription Factors
  • Ubiquitin
  • Ubiquitin-Conjugating Enzymes