Acetylation and MAPK phosphorylation cooperate to regulate the degradation of active GATA-1

Angel Hernandez-Hernandez, Pampa Ray, Gabi Litos, Marco Ciro, Sergio Ottolenghi, Hartmut Beug, Joan Boyes

Research output: Contribution to journalArticlepeer-review


Regulation of transcription requires mechanisms to both activate and terminate transcription factor activity. GATA-1 is a key haemopoietic transcription factor whose activity is increased by acetylation. We show here that acetylated GATA-1 is targeted for degradation via the ubiquitin/proteasome pathway. Acetylation positively signals ubiquitination, suggesting that activation by acetylation simultaneously marks GATA-1 for degradation. Promoter-specific MAPK phosphorylation then cooperates with acetylation to execute protein loss. The requirement for both modifications is novel and suggests a way by which degradation of the active protein can be specifically regulated in response to external phosphorylation-mediated signalling. As many transcription factors are activated by acetylation, we suggest that this might be a general mechanism to control transcription factor activity.

Original languageEnglish
Pages (from-to)3264-3274
Number of pages11
JournalEMBO Journal
Issue number14
Publication statusPublished - Jul 26 2006


  • Acetylation
  • Haemopoiesis
  • Phosphorylation
  • Transcription
  • Ubiquitination

ASJC Scopus subject areas

  • Genetics
  • Cell Biology


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