The transcriptional activation function of the HIF-like factor requires phosphorylation at a conserved threonine

Katarina Gradin, Chikahisa Takasaki, Yoshiaki Fujii-Kuriyama, Kazuhiro Sogawa

    Research output: Contribution to journalArticlepeer-review

    69 Citations (Scopus)

    Abstract

    The hypoxia-inducible factor (HIF)-1α and the HIF-like factor (HLF) transcription factors are regulated at multiple levels including protein stabilization, nuclear import, and activation of transactivation, resulting in recruitment of coactivators such as the cAMP-response element-binding protein (CREB)-binding protein (CBP)/ p300 and SRC-1. During low oxygen tension these proteins modulate a network of genes that are necessary for angiogenesis, erythropopoiesis, and glycolysis. We report here that the C-terminal transactivation domain of HLF is phosphorylated on multiple sites and that phosphorylation on threonine 844 of HLF is necessary for the transcriptional activation function of the protein independently of the hypoxia condition. Importantly, using the mammalian two-hybrid system we demonstrate that a substitution of threonine 844 to an alanine decreased the enhanced transcriptional activation function mediated by CBP/p300.

    Original languageEnglish
    Pages (from-to)23508-23514
    Number of pages7
    JournalJournal of Biological Chemistry
    Volume277
    Issue number26
    DOIs
    Publication statusPublished - 2002 Jun 28

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Fingerprint Dive into the research topics of 'The transcriptional activation function of the HIF-like factor requires phosphorylation at a conserved threonine'. Together they form a unique fingerprint.

    Cite this