Biology:ID1

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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

DNA-binding protein inhibitor ID-1 is a protein that in humans is encoded by the ID1 gene.[1][2]

Function

The protein encoded by this gene is a helix-loop-helix (HLH) protein that can form heterodimers with members of the basic HLH family of transcription factors.[1] The encoded protein has no DNA binding activity and therefore can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts.[1] This protein may play a role in cell growth, senescence, and differentiation.[3][4][5] Two transcript variants encoding different isoforms have been found for this gene.[6]

Interactions

ID1 has been shown to interact weakly with MyoD[1][7][8][9][10][11][12] but very tightly with ubiquitously expressed E proteins.[13] E proteins heterodimerize with tissue restricted bHLH proteins such as Myod, NeuroD, etc. to form active transcription complexes so by sequestering E proteins, Id proteins can inhibit tissue restricted gene expression in multiple cell lineages using the same biochemical mechanism. Other interacting partners include CASK.[14]

Clinical significance

ID1 can be used to mark endothelial progenitor cells which are critical to tumor growth and angiogenesis.[15][16] Targeting ID1 results in decreased tumor growth.[17][18] ID1 has been shown to be targeted by cannabidiol in certain gliomas and breast cancers.[19][20]

See also

References

  1. ↑ 1.0 1.1 1.2 1.3 "The protein Id: a negative regulator of helix-loop-helix DNA binding proteins". Cell 61 (1): 49–59. April 1990. doi:10.1016/0092-8674(90)90214-Y. PMID 2156629. 
  2. ↑ "Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts". The Journal of Biological Chemistry 269 (3): 2139–45. January 1994. doi:10.1016/S0021-9258(17)42146-6. PMID 8294468. 
  3. ↑ "Id proteins in development, cell cycle and cancer". Trends in Cell Biology 13 (8): 410–8. August 2003. doi:10.1016/S0962-8924(03)00147-8. PMID 12888293. 
  4. ↑ "Id family of helix-loop-helix proteins in cancer". Nature Reviews. Cancer 5 (8): 603–14. August 2005. doi:10.1038/nrc1673. PMID 16034366. 
  5. ↑ "Id genes are essential for early heart formation". Genes & Development 31 (13): 1325–1338. July 2017. doi:10.1101/gad.300400.117. PMID 28794185. 
  6. ↑ "Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3397. 
  7. ↑ "The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis". Nature 428 (6980): 328–32. March 2004. doi:10.1038/nature02329. PMID 15029197. Bibcode: 2004Natur.428..328G. 
  8. ↑ "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". The Journal of Biological Chemistry 272 (32): 19785–93. August 1997. doi:10.1074/jbc.272.32.19785. PMID 9242638. 
  9. ↑ "Detection and modulation in vivo of helix-loop-helix protein-protein interactions". The Journal of Biological Chemistry 268 (1): 5–8. January 1993. doi:10.1016/S0021-9258(18)54105-3. PMID 8380166. 
  10. ↑ "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene 16 (9): 1149–59. March 1998. doi:10.1038/sj.onc.1201634. PMID 9528857. 
  11. ↑ "The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein". The Journal of Biological Chemistry 277 (40): 37045–53. October 2002. doi:10.1074/jbc.M203336200. PMID 12145280. 
  12. ↑ "Id-1 induces proteasome-dependent degradation of the HBX protein". Journal of Molecular Biology 382 (1): 34–43. September 2008. doi:10.1016/j.jmb.2007.06.020. PMID 18674781. 
  13. ↑ "Overexpression of Id protein inhibits the muscle differentiation program: in vivo association of Id with E2A proteins". Genes & Development 6 (8): 1466–79. August 1992. doi:10.1101/gad.6.8.1466. PMID 1644289. 
  14. ↑ "CASK inhibits ECV304 cell growth and interacts with Id1". Biochemical and Biophysical Research Communications 328 (2): 517–21. March 2005. doi:10.1016/j.bbrc.2005.01.014. PMID 15694377. 
  15. ↑ "Id1 and Id3 are required for neurogenesis, angiogenesis and vascularization of tumour xenografts". Nature 401 (6754): 670–7. October 1999. doi:10.1038/44334. PMID 10537105. Bibcode: 1999Natur.401..670L. 
  16. ↑ "Impaired recruitment of bone-marrow-derived endothelial and hematopoietic precursor cells blocks tumor angiogenesis and growth". Nature Medicine 7 (11): 1194–201. November 2001. doi:10.1038/nm1101-1194. PMID 11689883. 
  17. ↑ "Peptide-conjugated antisense oligonucleotides for targeted inhibition of a transcriptional regulator in vivo". Nature Biotechnology 26 (1): 91–100. January 2008. doi:10.1038/nbt1366. PMID 18176556. 
  18. ↑ "Using the transcription factor inhibitor of DNA binding 1 to selectively target endothelial progenitor cells offers novel strategies to inhibit tumor angiogenesis and growth". Cancer Research 70 (18): 7273–82. September 2010. doi:10.1158/0008-5472.CAN-10-1142. PMID 20807818. 
  19. ↑ "Therapeutic reversal of prenatal pontine ID1 signaling in DIPG". Neuro Oncol 23 (supplement 1): i48. June 2021. doi:10.1093/neuonc/noab090.193. 
  20. ↑ "Cannabidiol as a novel inhibitor of Id-1 gene expression in aggressive breast cancer cells". Molecular Cancer Therapeutics 6 (11): 2921–7. November 2007. doi:10.1158/1535-7163.MCT-07-0371. PMID 18025276. 

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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