Biology:PRRX1
 Generic protein structure example |
Paired related homeobox 1 is a protein that in humans is encoded by the PRRX1 gene.[1][2]
Function
The DNA-associated protein encoded by this gene is a member of the paired family of homeobox proteins localized to the nucleus. The protein functions as a transcription coactivator, enhancing the DNA-binding activity of serum response factor, a protein required for the induction of genes by growth and differentiation factors. The protein regulates muscle creatine kinase, indicating a role in the establishment of diverse mesodermal muscle types. Alternative splicing yields two isoforms that differ in abundance and expression patterns.[2]
Role in mesenchymal stem cell differentiation
Prrx1 expression is restricted to the mesoderm during embryonic development, and both Prrx1 and Prrx2 are expressed in mesenchymal tissues in adult mice.[3][4][5][6][7] Mice that lack both Prrx1 and Prrx2 have profound defects in mesenchymal cell differentiation in the craniofacial region.[5][8] Several recent studies demonstrate that PRRX1 can regulate differentiation of mesenchymal precursors. For example, PRRX1 inhibits adipogenesis by activating transforming growth factor-beta (TGF-beta) signaling,[9] and also acts downstream of tumor necrosis factor-alpha to inhibit osteoblast differentiation.[10]
References
- ↑ "Human and Drosophila homeodomain proteins that enhance the DNA-binding activity of serum response factor". Science 257 (5073): 1089–95. Sep 1992. doi:10.1126/science.257.5073.1089. PMID 1509260. Bibcode: 1992Sci...257.1089G.
- ↑ 2.0 2.1 "Entrez Gene: PRRX1 paired related homeobox 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5396.
- ↑ "A novel murine homeobox gene isolated by a tissue specific PCR cloning strategy". Nucleic Acids Res. 20 (19): 5189–95. October 1992. doi:10.1093/nar/20.19.5189. PMID 1383943.
- ↑ "A chicken homeobox gene related to Drosophila paired is predominantly expressed in the developing limb". Dev. Biol. 158 (1): 254–64. July 1993. doi:10.1006/dbio.1993.1184. PMID 8101172.
- ↑ 5.0 5.1 "prx-1 functions cooperatively with another paired-related homeobox gene, prx-2, to maintain cell fates within the craniofacial mesenchyme". Development 126 (3): 495–504. February 1999. doi:10.1242/dev.126.3.495. PMID 9876178. http://dev.biologists.org/content/126/3/495.full.pdf.
- ↑ "Expression of rat homeobox gene, rHOX, in developing and adult tissues in mice and regulation of its mRNA expression in osteoblasts by bone morphogenetic protein 2 and parathyroid hormone-related protein". Mol. Endocrinol. 12 (11): 1721–32. November 1998. doi:10.1210/mend.12.11.0195. PMID 9817598.
- ↑ "MHox: a mesodermally restricted homeodomain protein that binds an essential site in the muscle creatine kinase enhancer". Development 115 (4): 1087–101. August 1992. doi:10.1242/dev.115.4.1087. PMID 1360403.
- ↑ "Prx1 and Prx2 in skeletogenesis: roles in the craniofacial region, inner ear and limbs". Development 125 (19): 3831–42. October 1998. doi:10.1242/dev.125.19.3831. PMID 9729491.
- ↑ "The transcription factor paired-related homeobox 1 (Prrx1) inhibits adipogenesis by activating transforming growth factor-β (TGFβ) signaling". J. Biol. Chem. 288 (5): 3036–47. February 2013. doi:10.1074/jbc.M112.440370. PMID 23250756.
- ↑ "Identification of the homeobox protein Prx1 (MHox, Prrx-1) as a regulator of osterix expression and mediator of tumor necrosis factor α action in osteoblast differentiation". J. Bone Miner. Res. 26 (1): 209–19. January 2011. doi:10.1002/jbmr.203. PMID 20683885.
Further reading
- "Sequence-specific targeting of nuclear signal transduction pathways by homeodomain proteins". Mol. Cell. Biol. 15 (6): 3318–26. 1995. doi:10.1128/MCB.15.6.3318. PMID 7760827.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I". Genes Dev. 11 (19): 2482–93. October 1997. doi:10.1101/gad.11.19.2482. PMID 9334314.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "NUP98 is fused to PMX1 homeobox gene in human acute myelogenous leukemia with chromosome translocation t(1;11)(q23;p15)". Blood 94 (2): 741–7. 1999. doi:10.1182/blood.V94.2.741. PMID 10397741.
- "A set of Hox proteins interact with the Maf oncoprotein to inhibit its DNA binding, transactivation, and transforming activities". J. Biol. Chem. 276 (1): 819–26. 2001. doi:10.1074/jbc.M007643200. PMID 11036080.
- "Human PRRX1 and PRRX2 genes: cloning, expression, genomic localization, and exclusion as disease genes for Nager syndrome". Mamm. Genome 11 (11): 1000–5. November 2000. doi:10.1007/s003350010193. PMID 11063257.
- "Prx1 controls vascular smooth muscle cell proliferation and tenascin-C expression and is upregulated with Prx2 in pulmonary vascular disease". Circ. Res. 89 (2): 131–8. July 2001. doi:10.1161/hh1401.093582. PMID 11463719.
- "HIV-1 Tat reprograms immature dendritic cells to express chemoattractants for activated T cells and macrophages". Nat. Med. 9 (2): 191–7. February 2003. doi:10.1038/nm822. PMID 12539042.
- "The high-mobility-group domain of Sox proteins interacts with DNA-binding domains of many transcription factors". Nucleic Acids Res. 34 (6): 1735–44. 2006. doi:10.1093/nar/gkl105. PMID 16582099.
- "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. May 2006. doi:10.1038/nature04727. PMID 16710414. Bibcode: 2006Natur.441..315G.
- "Human prx1 gene is a target of Nrf2 and is up-regulated by hypoxia/reoxygenation: implication to tumor biology". Cancer Res. 67 (2): 546–54. January 2007. doi:10.1158/0008-5472.CAN-06-2401. PMID 17234762.
External links
- PRRX1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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