ID1
DNA-binding protein inhibitor ID-1 is a protein that in mice and humans (and other vertebrates) is encoded by the ID1 gene.[1][2]. 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]
Contents |
[edit] 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]
[edit] Clinical significance
ID1 can be used to mark endothelial progenitor cells which are critical to tumour growth and angiogenesis[14][15]. Targeting ID1 results in decreased tumour growth [16]. Therefore, ID1 could be used to design a novel cancer therapy.[16][17]
[edit] References
- ^ a b c d Benezra R, Davis RL, Lockshon D and 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, Oda K (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, M and 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, and 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". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3397.
- ^ Garkavtsev, Igor; Kozin Sergey V, Chernova Olga, Xu Lei, Winkler Frank, Brown Edward, Barnett Gene H, Jain Rakesh K (March 2004). "The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis". Nature (England) 428 (6980): 328–332. doi:10.1038/nature02329. PMID 15029197.
- ^ Langlands, K; Yin X, Anand G, Prochownik E V (August 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. (UNITED STATES) 272 (32): 19785–19793. doi:10.1074/jbc.272.32.19785. ISSN 0021-9258. PMID 9242638.
- ^ Finkel, T; Duc J, Fearon E R, Dang C V, Tomaselli G F (January 1993). "Detection and modulation in vivo of helix-loop-helix protein-protein interactions". J. Biol. Chem. (UNITED STATES) 268 (1): 5–8. ISSN 0021-9258. PMID 8380166.
- ^ Gupta, K; Anand G, Yin X, Grove L, Prochownik E V (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene (ENGLAND) 16 (9): 1149–1159. doi:10.1038/sj.onc.1201634. ISSN 0950-9232. PMID 9528857.
- ^ McLoughlin, Patricia; Ehler Elisabeth, Carlile Graeme, Licht Jonathan D, Schäfer Beat W (October 2002). "The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein". J. Biol. Chem. (United States) 277 (40): 37045–37053. doi:10.1074/jbc.M203336200. ISSN 0021-9258. PMID 12145280.
- ^ Ling, Ming-Tat; Chiu Yung-Tuen, Lee Terence Kin Wah, Leung Steve Chin Lung, Fung Maggie Ka Lai, Wang Xianghong, Wong Kwong Fai, Wong Yong-Chuan (September 2008). "Id-1 induces proteasome-dependent degradation of the HBX protein". J. Mol. Biol. (England) 382 (1): 34–43. doi:10.1016/j.jmb.2007.06.020. PMID 18674781.
- ^ Jen Y, Weintraub, H and Benezra, R (1992). "Overexpression of Id protein inhibits the muscle differentiation program: In vivo association of Id with E2A proteins". Genes and Development 6 (8): 1466–79. doi:10.1101/gad.6.8.1466. PMID 1644289.
- ^ Qi, Jie; Su Yongyue, Sun Rongju, Zhang Fang, Luo Xiaofeng, Yang Zongcheng, Luo Xiangdong (March 2005). "CASK inhibits ECV304 cell growth and interacts with Id1". Biochem. Biophys. Res. Commun. (United States) 328 (2): 517–521. doi:10.1016/j.bbrc.2005.01.014. ISSN 0006-291X. PMID 15694377.
- ^ Lyden D et al (1999). "Id1 and Id3 are required for neurogenesis,angiogenesis and vascularization of tumor xenografts". Nature 401 (6754): 670–677. doi:10.1038/44334. PMID 10537105.
- ^ Lyden D et al (2001). "Impaired recruitment of bone-marrow-derived endothelial and hematopoietic precursor cells blocks tumor angiogenesis and growth". Nature Biotechnology 7 (11): 1194–1201. doi:10.1038/nm1101-1194. PMID 11689883.
- ^ a b >Henke E et al (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.
- ^ Mellick As, Plummer PN et al (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): 7273–7282. doi:10.1158/0008-5472.CAN-10-1142. PMC 3058751. PMID 20807818. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3058751.
[edit] See also
[edit] Further reading
- Zhu W, Dahmen J, Bulfone A 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. PMID 8086456.
- Mathew S, Chen W, Murty VV et al (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 et al (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 et al (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 et al (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171189.
- Outinen PA, Sood SK, Pfeifer SI 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 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 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=311163.
- 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 et al (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.
- Deloukas P, Matthews LH, Ashurst J et al (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133750.
- Ouyang XS, Wang X, Ling MT et al (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. PMID 12020803.
- Wang X, Xu K, Ling MT 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.
[edit] External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
|
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| This article on a gene on chromosome 20 is a stub. You can help Wikipedia by expanding it. |