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ID1

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This article is about the protein. For other uses, see ID1 (disambiguation).
ID1
Identifiers
AliasesID1, ID, bHLHb24, inhibitor of DNA binding 1, HLH protein
External IDsOMIM: 600349; MGI: 96396; HomoloGene: 1631; GeneCards: ID1; OMA:ID1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

3397

15901

Ensembl

ENSG00000125968

ENSMUSG00000042745

UniProt

P41134

P20067
Q6GTZ3

RefSeq (mRNA)

NM_181353
NM_002165

NM_010495
NM_001355113
NM_001369018

RefSeq (protein)

NP_002156
NP_851998

NP_034625
NP_001342042
NP_001355947

Location (UCSC)Chr 20: 31.61 – 31.61 MbChr 2: 152.58 – 152.58 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DNA-binding protein inhibitor ID-1 is a protein that in humans is encoded by the ID1 gene.[5][6]

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.[5] 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.[5] This protein may play a role in cell growth, senescence, and differentiation.[7][8][9] Two transcript variants encoding different isoforms have been found for this gene.[10]

Interactions

ID1 has been shown to interact weakly with MyoD[5][11][12][13][14][15][16] but very tightly with ubiquitously expressed E proteins.[17] 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.[18]

Clinical significance

ID1 can be used to mark endothelial progenitor cells which are critical to tumor growth and angiogenesis.[19][20] Targeting ID1 results in decreased tumor growth.[21][22] ID1 has been shown to be targeted by cannabidiol in certain gliomas and breast cancers.[23][24]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000125968 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000042745 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c d Benezra R, Davis RL, Lockshon D, Turner DL, Weintraub H (April 1990). "The protein Id: a negative regulator of helix-loop-helix DNA binding proteins". Cell. 61 (1): 49–59. doi:10.1016/0092-8674(90)90214-Y. PMID 2156629. S2CID 29514374.
  6. ^ Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H, Oda K (January 1994). "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. doi:10.1016/S0021-9258(17)42146-6. PMID 8294468.
  7. ^ Ruzinova MB, Benezra R (August 2003). "Id proteins in development, cell cycle and cancer". Trends in Cell Biology. 13 (8): 410–8. doi:10.1016/S0962-8924(03)00147-8. PMID 12888293.
  8. ^ Perk J, Iavarone A, Benezra R (August 2005). "Id family of helix-loop-helix proteins in cancer". Nature Reviews. Cancer. 5 (8): 603–14. doi:10.1038/nrc1673. PMID 16034366. S2CID 19850793.
  9. ^ Cunningham TJ, Yu MS, McKeithan WL, Spiering S, Carrette F, Huang CT, et al. (July 2017). "Id genes are essential for early heart formation". Genes & Development. 31 (13): 1325–1338. doi:10.1101/gad.300400.117. PMC 5580654. PMID 28794185.
  10. ^ "Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein".
  11. ^ Garkavtsev I, Kozin SV, Chernova O, Xu L, Winkler F, Brown E, et al. (March 2004). "The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis". Nature. 428 (6980): 328–32. Bibcode:2004Natur.428..328G. doi:10.1038/nature02329. PMID 15029197. S2CID 4427531.
  12. ^ Langlands K, Yin X, Anand G, Prochownik EV (August 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". The Journal of Biological Chemistry. 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. PMID 9242638.
  13. ^ Finkel T, Duc J, Fearon ER, Dang CV, Tomaselli GF (January 1993). "Detection and modulation in vivo of helix-loop-helix protein-protein interactions". The Journal of Biological Chemistry. 268 (1): 5–8. doi:10.1016/S0021-9258(18)54105-3. PMID 8380166.
  14. ^ Gupta K, Anand G, Yin X, Grove L, Prochownik EV (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene. 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.
  15. ^ McLoughlin P, Ehler E, Carlile G, Licht JD, Schäfer BW (October 2002). "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. doi:10.1074/jbc.M203336200. PMID 12145280.
  16. ^ Ling MT, Chiu YT, Lee TK, Leung SC, Fung MK, Wang X, et al. (September 2008). "Id-1 induces proteasome-dependent degradation of the HBX protein". Journal of Molecular Biology. 382 (1): 34–43. doi:10.1016/j.jmb.2007.06.020. PMID 18674781.
  17. ^ Jen Y, Weintraub H, Benezra R (August 1992). "Overexpression of Id protein inhibits the muscle differentiation program: in vivo association of Id with E2A proteins". Genes & Development. 6 (8): 1466–79. doi:10.1101/gad.6.8.1466. PMID 1644289.
  18. ^ Qi J, Su Y, Sun R, Zhang F, Luo X, Yang Z, Luo X (March 2005). "CASK inhibits ECV304 cell growth and interacts with Id1". Biochemical and Biophysical Research Communications. 328 (2): 517–21. doi:10.1016/j.bbrc.2005.01.014. PMID 15694377.
  19. ^ Lyden D, Young AZ, Zagzag D, Yan W, Gerald W, O'Reilly R, et al. (October 1999). "Id1 and Id3 are required for neurogenesis, angiogenesis and vascularization of tumour xenografts". Nature. 401 (6754): 670–7. Bibcode:1999Natur.401..670L. doi:10.1038/44334. PMID 10537105. S2CID 4396535.
  20. ^ Lyden D, Hattori K, Dias S, Costa C, Blaikie P, Butros L, et al. (November 2001). "Impaired recruitment of bone-marrow-derived endothelial and hematopoietic precursor cells blocks tumor angiogenesis and growth". Nature Medicine. 7 (11): 1194–201. doi:10.1038/nm1101-1194. PMID 11689883. S2CID 12961562.
  21. ^ Henke E, Perk J, Vider J, de Candia P, Chin Y, Solit DB, et al. (January 2008). "Peptide-conjugated antisense oligonucleotides for targeted inhibition of a transcriptional regulator in vivo". Nature Biotechnology. 26 (1): 91–100. doi:10.1038/nbt1366. PMID 18176556. S2CID 205273623.
  22. ^ Mellick AS, Plummer PN, Nolan DJ, Gao D, Bambino K, Hahn M, et al. (September 2010). "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. doi:10.1158/0008-5472.CAN-10-1142. PMC 3058751. PMID 20807818.
  23. ^ Yadav VN, Harris MK, Messinger D, Thomas C, Cummings JR, Yang T, Woo R, Siddaway R, Burkert M, Stallard S, Qin T (June 2021). "Therapeutic reversal of prenatal pontine ID1 signaling in DIPG". Neuro Oncol. 23 (supplement 1): i48. doi:10.1093/neuonc/noab090.193. PMC 8168201.
  24. ^ McAllister SD, Christian RT, Horowitz MP, Garcia A, Desprez PY (November 2007). "Cannabidiol as a novel inhibitor of Id-1 gene expression in aggressive breast cancer cells". Molecular Cancer Therapeutics. 6 (11): 2921–7. doi:10.1158/1535-7163.MCT-07-0371. PMID 18025276. S2CID 2192838.

Further reading

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

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