Soufi, Abdenour and Jayaraman, Padma-Sheela (2008) PRH/Hex: an oligomeric transcription factor and ,ultifunctional regulator of cell fate. Biochemical Journal, 412 (3). pp. 399-413. ISSN 0264-6021
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| URL of Published Version: http://www.biochemj.org/bj/412/0399/4120399.pdf Identification Number/DOI: 10.1042/BJ20080035 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 DNAbinding 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. |
| Type of Work: | Article |
|---|---|
| Date: | 28 May 2008 (Publication) |
| School/Faculty: | Schools (1998 to 2008) > School of Medicine |
| Department: | Division of Immunity and Infection |
| Subjects: | R Medicine (General) |
| Institution: | University of Birmingham |
| Copyright Holders: | Portland Press |
| ID Code: | 127 |
| Refereed: | YES |
| Local Holdings: |
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