Title | PRH/Hex: an oligomeric transcription factor and multifunctional regulator of cell fate. |
Publication Type | Journal Article |
Year of Publication | 2008 |
Authors | Soufi A, Jayaraman P-S |
Journal | Biochem J |
Volume | 412 |
Issue | 3 |
Pagination | 399-413 |
Date Published | 2008 Jun 15 |
ISSN | 1470-8728 |
Keywords | Amino Acid Sequence, Animals, Avian Proteins, Cell Proliferation, Dimerization, Homeodomain Proteins, Humans, Models, Biological, Molecular Sequence Data, Protein Structure, Tertiary, Sequence Alignment, Transcription Factors, Transcription, Genetic |
Abstract | The PRH (proline-rich homeodomain) [also known as Hex (haematopoietically expressed homeobox)] protein is a critical regulator of vertebrate development. PRH is able to regulate cell proliferation and differentiation and is required for the formation of the vertebrate body axis, the haematopoietic and vascular systems and the formation of many vital organs. PRH is a DNA-binding protein that can repress and activate the transcription of its target genes using multiple mechanisms. In addition, PRH can regulate the nuclear transport of specific mRNAs making PRH a member of a select group of proteins that control gene expression at the transcriptional and translational levels. Recent biophysical analysis of the PRH protein has shown that it forms homo-oligomeric complexes in vivo and in vitro and that the proline-rich region of PRH forms a novel dimerization interface. Here we will review the current literature on PRH and discuss the complex web of interactions centred on this multifunctional protein. |
DOI | 10.1042/BJ20080035 |
Alternate Journal | Biochem. J. |
PubMed ID | 18498250 |
PubMed Central ID | PMC2570084 |