Biology:HHEX

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Hematopoietically-expressed homeobox protein HHEX is a protein that in humans is encoded by the HHEX gene and also known as Proline Rich Homeodomain protein PRH.[1][2][3]

This gene encodes a member of the homeobox family of transcription factors, many of which are involved in developmental processes. Expression in specific hematopoietic lineages suggests that this protein may play a role in hematopoietic differentiation but the expression of this protein is not limited to hematopoietic cells.[3]

Function

The HHEX transcription factor acts as a activator of transcription in some instances and a repressor of transcription others.[4][5] It interacts with a number of other signaling molecules to play an important role in the development of multiple organs, such as the liver, thyroid and forebrain.[6] HHEX serves to repress VEGFA, another protein which is important in endothelial cell development.[7] SCL, a significant transcription factor for blood and endothelial cell differentiation, is shown to interact with HHEX to promote the correct development of the hematopoiesis process.[8] HHEX appears to work together with another molecule, β-catenin, for the development of the anterior organizer.[9] It also contributes to developmental remodeling and stabilization of endothelial cells in an unborn organism.[7] The importance of this transcription factor is illustrated by the inability of HHEX knockout mice embryos to survive gestation. Without the expression of HHEX, these mice embryos die in utero between Day 13 and Day 16.[7] HHEX knockout mice display a range of abnormalities including forebrain abnormalities in various levels of severity, as well as a number of other defects including heart, vasculature, liver, monocyte, and thyroid abnormalities.[6][7] The HHEX protein is important in a variety of cancers and it can act as an tumour suppressor protein or as an oncoprotein depending on the cancer type.

Interactions

HHEX has been shown to interact with Promyelocytic leukemia protein.[10]

References

  1. ↑ "HEX: a novel homeobox gene expressed during haematopoiesis and conserved between mouse and human". Nucleic Acids Research 21 (5): 1245–9. Mar 1993. doi:10.1093/nar/21.5.1245. PMID 8096636. 
  2. ↑ "PCR cloning of an orphan homeobox gene (PRH) preferentially expressed in myeloid and liver cells". Biochemical and Biophysical Research Communications 195 (2): 976–83. Sep 1993. doi:10.1006/bbrc.1993.2140. PMID 8103988. 
  3. ↑ 3.0 3.1 "Entrez Gene: HHEX hematopoietically expressed homeobox". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3087. 
  4. ↑ "Divergent homeobox gene hex regulates promoter of the Na(+)-dependent bile acid cotransporter". American Journal of Physiology. Gastrointestinal and Liver Physiology 279 (2): G347-55. Aug 2000. doi:10.1152/ajpgi.2000.279.2.G347. PMID 10915644. 
  5. ↑ "Hex is a transcriptional repressor that contributes to anterior identity and suppresses Spemann organiser function". Development 127 (11): 2303–15. Jun 2000. doi:10.1242/dev.127.11.2303. PMID 10804173. http://dev.biologists.org/content/127/11/2303.abstract. 
  6. ↑ 6.0 6.1 "The homeobox gene Hex is required in definitive endodermal tissues for normal forebrain, liver and thyroid formation". Development 127 (11): 2433–45. Jun 2000. doi:10.1242/dev.127.11.2433. PMID 10804184. https://discovery.ucl.ac.uk/id/eprint/10090339/. 
  7. ↑ 7.0 7.1 7.2 7.3 "A null mutation of Hhex results in abnormal cardiac development, defective vasculogenesis and elevated Vegfa levels". Development 131 (20): 5197–209. Oct 2004. doi:10.1242/dev.01393. PMID 15459110. 
  8. ↑ "Hhex and scl function in parallel to regulate early endothelial and blood differentiation in zebrafish". Development 127 (20): 4303–13. Oct 2000. doi:10.1242/dev.127.20.4303. PMID 11003831. 
  9. ↑ "Hex acts with beta-catenin to regulate anteroposterior patterning via a Groucho-related co-repressor and Nodal". Development 133 (18): 3709–22. Sep 2006. doi:10.1242/dev.02516. PMID 16936074. 
  10. ↑ "The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control". Oncogene 18 (50): 7091–100. Nov 1999. doi:10.1038/sj.onc.1203201. PMID 10597310. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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