Journal
EMBO REPORTS
Volume 12, Issue 10, Pages 1018-1023Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/embor.2011.152
Keywords
Krox20; Nab; SUMO ligase; Ubc9
Categories
Funding
- JAE
- JAE intro (CSIC)
- MICINN [BFU2009-10986/BMC]
- CSIC [200920I085]
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Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins regulates many processes in the eukaryotic cell. This reaction is similar to ubiquitination and usually requires an E3 ligase for substrate modification. However, only a few SUMO ligases have been described so far, which frequently facilitate sumoylation by bringing together the SUMO-conjugating enzyme Ubc9 and the target protein. Ubc9 is an interaction partner of the transcription factor Krox20, a key regulator of hindbrain development. Here, we show that Krox20 functions as a SUMO ligase for its coregulators-the Nab proteins-and that Nab sumoylation negatively modulates Krox20 transcriptional activity in vivo.
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