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Filamin A-bound PEBP2beta/CBFbeta is retained in the cytoplasm and prevented from functioning as a partner of the Runx1 transcription factor.
- Source :
-
Molecular and cellular biology [Mol Cell Biol] 2005 Feb; Vol. 25 (3), pp. 1003-12. - Publication Year :
- 2005
-
Abstract
- The heterodimeric transcription factor PEBP2/CBF is composed of a DNA-binding subunit, called Runx1, and a non-DNA-binding subunit, called PEBP2beta/CBFbeta. The Runx1 protein is detected exclusively in the nuclei of most cells and tissues, whereas PEBP2beta is located in the cytoplasm. We addressed the mechanism by which PEBP2beta localizes to the cytoplasm and found that it is associated with filamin A, an actin-binding protein. Filamin A retains PEBP2beta in the cytoplasm, thereby hindering its engagement as a Runx1 partner. The interaction with filamin A is mediated by a region within PEBP2beta that includes amino acid residues 68 to 93. The deletion of this region or the repression of filamin A enables PEBP2beta to translocate to the nucleus. Based on these observations, we propose that PEBP2beta has two distinct domains, a newly defined regulatory domain that interacts with filamin A and the previously identified Runx1-binding domain.
- Subjects :
- Animals
Core Binding Factor Alpha 2 Subunit
Filamins
HeLa Cells
Humans
Mice
Protein Binding
Protein Structure, Tertiary
RNA, Small Interfering metabolism
Transcription Factor AP-2
Two-Hybrid System Techniques
Cell Nucleus metabolism
Contractile Proteins metabolism
Cytoplasm metabolism
DNA-Binding Proteins metabolism
Microfilament Proteins metabolism
Proto-Oncogene Proteins metabolism
Transcription Factors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0270-7306
- Volume :
- 25
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Molecular and cellular biology
- Publication Type :
- Academic Journal
- Accession number :
- 15657428
- Full Text :
- https://doi.org/10.1128/MCB.25.3.1003-1012.2005