Msh homeobox 2

From Wikipedia, the free encyclopedia
AliasesMSX2, CRS2, FPP, HOX8, MSH, PFM, PFM1, Msh homeobox 2
External IDsOMIM: 123101 MGI: 97169 HomoloGene: 1837 GeneCards: MSX2
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 5: 174.72 – 174.73 Mbn/a
PubMed search[2][3]
View/Edit HumanView/Edit Mouse

Homeobox protein MSX-2 is a protein that in humans is encoded by the MSX2 gene.[4][5][6]


This gene encodes a member of the muscle segment homeobox gene family. The encoded protein is a transcriptional repressor whose normal activity may establish a balance between survival and apoptosis of neural crest-derived cells required for proper craniofacial morphogenesis. The encoded protein may also have a role in promoting cell growth under certain conditions and may be an important target for the RAS signaling pathways. Mutations in this gene are associated with parietal foramina 1 and craniosynostosis type 2.[6] Msx2 is a homeobox gene localized on human chromosome 5 that encodes a transcription repressor and activator (MSX-2) responsible for craniofacial and limb-bud development. Cells will express msx2 when exposed to signaling molecules BMP-2 and BMP-4 in situ.[7] Expression of msx2 leads to the proliferation, migration and osteogenic differentiation of neural crest cells during embryogenesis and bone fracture.[8] It is well documented that expression of cell-cell adhesion molecules such as E-cadherins will promote structural integrity and an epithelial arrangement of cells, while expression of N-cadherin and vimentin promote mesenchymal arrangement and cell migration.[9][10] Msx2 downregulates E-cadherins and upregulates N-cadherin and vimentin which indicates its role in inducing epithelial mesenchymal transition (EMT). Germline knockout mice have been created for this gene (Msx2 +/-) in order to examine functional loss.[11] Clinical studies on craniosynostosis, or the premature fusion of cranial structures, have shown the condition to be genetically linked to mutation in the msx2 homeobox gene.[12]


Msh homeobox 2 has been shown to interact with DLX5,[13] DLX2[13] and MSX1.[13]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000120149Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Takahashi C, Akiyama N, Matsuzaki T, Takai S, Kitayama H, Noda M (May 1996). "Characterization of a human MSX-2 cDNA and its fragment isolated as a transformation suppressor gene against v-Ki-ras oncogene". Oncogene. 12 (10): 2137–46. PMID 8668339.
  5. ^ Kostrzewa M, Grady DL, Moyzis RK, Flöter L, Müller U (March 1996). "Integration of four genes, a pseudogene, thirty-one STSs, and a highly polymorphic STRP into the 7-10 Mb YAC contig of 5q34-q35". Human Genetics. 97 (3): 399–403. doi:10.1007/BF02185781. PMID 8786091. S2CID 12647370.
  6. ^ a b "Entrez Gene: MSX2 msh homeobox 2".
  7. ^ Rifas L (July 1997). "Gestational exposure to ethanol suppresses msx2 expression in developing mouse embryos". Proc Natl Acad Sci U S A. 94 (14): 7549–54. Bibcode:1997PNAS...94.7549R. doi:10.1073/pnas.94.14.7549. PMC 23859. PMID 9207129.
  8. ^ Liu H, Chen B, Li Y (March 2019). "microRNA-203 promotes proliferation, differentiation, and migration of osteoblasts by upregulation of Msh homeobox 2". Journal of Cellular Physiology. 234 (10): 17639–17648. doi:10.1002/jcp.28387. PMID 30854680. S2CID 73726197.
  9. ^ Fujita T, Hayashida K, Shiba H, Kishimoto A, Matsuda S, Takeda K, Kawaguchi H, Kurihara H (August 2010). "The expressions of claudin-1 and E-cadherin in junctional epithelium". Journal of Periodontal Research. 45 (4): 579–82. doi:10.1111/j.1600-0765.2009.01258.x. PMID 20337884.
  10. ^ Zhao Y, Yao J, Wu XP, Zhao L, Zhou YX, Zhang Y, You QD, Guo QL, Lu N (June 2015). "Wogonin suppresses human alveolar adenocarcinoma cell A549 migration in inflammatory microenvironment by modulating the IL-6/STAT3 signaling pathway". Molecular Carcinogenesis. 54 (Suppl 1): E81-93. doi:10.1002/mc.22182. PMID 24976450. S2CID 29685898.
  11. ^ Yu Z, Yu W, Liu J, Wu D, Wang C, Zhang J, Zhao J (July 2018). "Lens-specific deletion of the Msx2 gene increased apoptosis by enhancing the caspase-3/caspase-8 signaling pathway". The Journal of International Medical Research. 46 (7): 2843–2855. doi:10.1177/0300060518774687. PMC 6124292. PMID 29921154.
  12. ^ Melville H, Wang Y, Taub PJ, Jabs EW (December 2010). "Genetic basis of potential therapeutic strategies for craniosynostosis". American Journal of Medical Genetics. Part A. 152A (12): 3007–15. doi:10.1002/ajmg.a.33703. PMID 21082653. S2CID 24424024.
  13. ^ a b c Zhang H, Hu G, Wang H, Sciavolino P, Iler N, Shen MM, Abate-Shen C (May 1997). "Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism". Molecular and Cellular Biology. 17 (5): 2920–32. doi:10.1128/mcb.17.5.2920. PMC 232144. PMID 9111364.

Further reading[edit]

External links[edit]

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