DNA-binding protein inhibitor ID-1 is a protein that in humans is encoded by the ID1 gene.[1][2]
Contents
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] Two transcript variants encoding different isoforms have been found for this gene.[5]
Interactions
ID1 has been shown to interact weakly with MyoD[1][6][7][8][9][10][11] but very tightly with ubiquitously expressed E proteins.[12] 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.[13]
Clinical significance
ID1 can be used to mark endothelial progenitor cells which are critical to tumor growth and angiogenesis.[14][15] Targeting ID1 results in decreased tumor growth.[16][17]
See also
References
- ^ a b c d Benezra R, Davis RL, Lockshon D, Turner DL, Weintraub H (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.
- ^ Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H et al. (February 1994). "Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts". J Biol Chem 269 (3): 2139–45. PMID 8294468.
- ^ Ruzinova MB, Benezra R (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.
- ^ Perk J, Iavarone A, Benezra R (2005). "The Id family of helix-loop-helix proteins in cancer". Nat Rev Cancer 5 (8): 603–614. doi:10.1038/nrc1673. PMID 16034366.
- ^ "Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein".
- ^ 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. doi:10.1038/nature02329. PMID 15029197.
- ^ Langlands K, Yin X, Anand G, Prochownik EV (August 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. PMID 9242638.
- ^ Finkel T, Duc J, Fearon ER, Dang CV, Tomaselli GF (January 1993). "Detection and modulation in vivo of helix-loop-helix protein-protein interactions". J. Biol. Chem. 268 (1): 5–8. PMID 8380166.
- ^ 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.
- ^ 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". J. Biol. Chem. 277 (40): 37045–53. doi:10.1074/jbc.M203336200. PMID 12145280.
- ^ 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". J. Mol. Biol. 382 (1): 34–43. doi:10.1016/j.jmb.2007.06.020. PMID 18674781.
- ^ 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 Dev. 6 (8): 1466–79. doi:10.1101/gad.6.8.1466. PMID 1644289.
- ^ Qi J, Su Y, Sun R, Zhang F, Luo X, Yang Z et al. (March 2005). "CASK inhibits ECV304 cell growth and interacts with Id1". Biochem. Biophys. Res. Commun. 328 (2): 517–21. doi:10.1016/j.bbrc.2005.01.014. PMID 15694377.
- ^ 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. doi:10.1038/44334. PMID 10537105.
- ^ 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". Nat. Med. 7 (11): 1194–201. doi:10.1038/nm1101-1194. PMID 11689883.
- ^ 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". Nat. Biotechnol. 26 (1): 91–100. doi:10.1038/nbt1366. PMID 18176556.
- ^ 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 tumour angiogenesis and growth". Cancer Res. 70 (18): 7273–82. doi:10.1158/0008-5472.CAN-10-1142. PMC 3058751. PMID 20807818.
Further reading
- Zhu W, Dahmen J, Bulfone A, Rigolet M, Hernandez MC, Kuo WL et al. (1995). "Id gene expression during development and molecular cloning of the human Id-1 gene". Brain Res. Mol. Brain Res. 30 (2): 312–26. doi:10.1016/0169-328X(95)00017-M. PMID 7637581.
- Deed RW, Jasiok M, Norton JD (1994). "Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins". Biochim. Biophys. Acta 1219 (1): 160–2. doi:10.1016/0167-4781(94)90261-5. PMID 8086456.
- Mathew S, Chen W, Murty VV, Benezra R, Chaganti RS (1996). "Chromosomal assignment of human ID1 and ID2 genes". Genomics 30 (2): 385–7. doi:10.1006/geno.1995.0037. PMID 8586447.
- Nehlin JO, Hara E, Kuo WL, Collins C, Campisi J (1997). "Genomic organization, sequence, and chromosomal localization of the human helix-loop-helix Id1 gene". Biochem. Biophys. Res. Commun. 231 (3): 628–34. doi:10.1006/bbrc.1997.6152. PMID 9070860.
- Anand G, Yin X, Shahidi AK, Grove L, Prochownik EV (1997). "Novel regulation of the helix-loop-helix protein Id1 by S5a, a subunit of the 26 S proteasome". J. Biol. Chem. 272 (31): 19140–51. doi:10.1074/jbc.272.31.19140. PMID 9235903.
- Langlands K, Yin X, Anand G, Prochownik EV (1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–19793. doi:10.1074/jbc.272.32.19785. PMID 9242638.
- Yates PR, Atherton GT, Deed RW, Norton JD, Sharrocks AD (1999). "Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors". EMBO J. 18 (4): 968–76. doi:10.1093/emboj/18.4.968. PMC 1171189. PMID 10022839.
- Outinen PA, Sood SK, Pfeifer SI, Pamidi S, Podor TJ, Li J et al. (1999). "Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells". Blood 94 (3): 959–67. PMID 10419887.
- Langlands K, Down GA, Kealey T (2000). "Id proteins are dynamically expressed in normal epidermis and dysregulated in squamous cell carcinoma". Cancer Res. 60 (21): 5929–33. PMID 11085505.
- Ohtani N, Zebedee Z, Huot TJ, Stinson JA, Sugimoto M, Ohashi Y et al. (2001). "Opposing effects of Ets and Id proteins on p16INK4a expression during cellular senescence". Nature 409 (6823): 1067–70. doi:10.1038/35059131. PMID 11234019.
- Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T et al. (2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.
- Korchynskyi O, ten Dijke P (2002). "Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter". J. Biol. Chem. 277 (7): 4883–4891. doi:10.1074/jbc.M111023200. PMID 11729207.
- Jögi A, Persson P, Grynfeld A, Påhlman S, Axelson H (2002). "Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation". J. Biol. Chem. 277 (11): 9118–26. doi:10.1074/jbc.M107713200. PMID 11756408.
- Singh J, Murata K, Itahana Y, Desprez PY (2002). "Constitutive expression of the Id-1 promoter in human metastatic breast cancer cells is linked with the loss of NF-1/Rb/HDAC-1 transcription repressor complex". Oncogene 21 (12): 1812–1822. doi:10.1038/sj.onc.1205252. PMID 11896613.
- Liu CJ, Ding B, Wang H, Lengyel P (2002). "The MyoD-inducible p204 protein overcomes the inhibition of myoblast differentiation by Id proteins". Mol. Cell. Biol. 22 (9): 2893–2905. doi:10.1128/MCB.22.9.2893-2905.2002. PMC 133750. PMID 11940648.
- Ouyang XS, Wang X, Ling MT, Wong HL, Tsao SW, Wong YC (2002). "Id-1 stimulates serum independent prostate cancer cell proliferation through inactivation of p16(INK4a)/pRB pathway". Carcinogenesis 23 (5): 721–5. doi:10.1093/carcin/23.5.721. PMID 12016143.
- Ling MT, Wang X, Tsao SW, Wong YC (2002). "Down-regulation of Id-1 expression is associated with TGF beta 1-induced growth arrest in prostate epithelial cells". Biochim. Biophys. Acta 1570 (3): 145–52. doi:10.1016/S0304-4165(02)00189-7. PMID 12020803.
- Wang X, Xu K, Ling MT, Wong YC, Feng HC, Nicholls J et al. (2002). "Evidence of increased Id-1 expression and its role in cell proliferation in nasopharyngeal carcinoma cells". Mol. Carcinog. 35 (1): 42–9. doi:10.1002/mc.10072. PMID 12203366.
External links
- ID1 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.