Two conserved domains in PCIF1 mediate interaction with pancreatic transcription factor PDX-1

Aihua Liu, Jennifer Oliver-Krasinski, Doris A. Stoffers

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


PCIF1 is a TRAF and POZ domain containing nuclear factor that interacts with and inhibits transactivation of pancreatic homeodomain transcription factor PDX-1. Here, we demonstrate interaction of endogenous PDX-1 and PCIF1 in MIN6 insulinoma cells. Within PCIF1, the TRAF and POZ domains are both required for physical and functional interaction with the C-terminus of PDX-1, whereas the C-terminal domain of PCIF1 directs its nuclear localization. A human PDX-1 mutation associated with diabetes, E224K, disrupts the ability of PCIF1 to inhibit PDX-1 transactivation, suggesting that the interaction between PDX-1 and PCIF1 is required for normal glucose homeostasis. Inhibition of transactivation occurs by a mechanism distinct from the classical role of POZ domains to recruit co-repressors and histone deacetylases. Understanding the functional roles of PCIF1 domains may have application to therapeutic β-cell replacement strategies involving PDX-1 for the treatment of diabetes.

Original languageEnglish (US)
Pages (from-to)6701-6706
Number of pages6
JournalFEBS Letters
Issue number28-29
StatePublished - Dec 11 2006
Externally publishedYes


  • Development
  • Diabetes
  • Insulin
  • Islet
  • MODY
  • Pancreas

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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