Filamin A-bound PEBP2β/CBFβ is retained in the cytoplasm and prevented from functioning as a partner of the Runx1 transcription factor

Naomi Yoshida, Takehiro Ogata, Kenji Tanabe, Songhua Li, Megumi Nakazato, Kazuyoshi Kohu, Toshiro Takafuta, Sandor Shapiro, Yasutaka Ohta, Masanobu Satake, Toshio Watanabe

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)

Abstract

The heterodimeric transcription factor PEBP2/CBF is composed of a DNA-binding subunit, called Runx1, and a non-DNA-binding subunit, called PEBP2β/CBFβ. The Runx1 protein is detected exclusively in the nuclei of most cells and tissues, whereas PEBP2β is located in the cytoplasm. We addressed the mechanism by which PEBP2β localizes to the cytoplasm and found that it is associated with filamin A, an actin-binding protein. Filamin A retains PEBP2β in the cytoplasm, thereby hindering its engagement as a Runx1 partner. The interaction with filamin A is mediated by a region within PEBP2β that includes amino acid residues 68 to 93. The deletion of this region or the repression of filamin A enables PEBP2β to translocate to the nucleus. Based on these observations, we propose that PEBP2β has two distinct domains, a newly defined regulatory domain that interacts with filamin A and the previously identified Runx1-binding domain.

Original languageEnglish
Pages (from-to)1003-1012
Number of pages10
JournalMolecular and cellular biology
Volume25
Issue number3
DOIs
Publication statusPublished - 2005 Feb

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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