ID2
DNA-binding protein inhibitor ID-2 is a protein that in humans is encoded by the ID2 gene.[5]
Function
The protein encoded by this gene belongs to the inhibitor of DNA binding (ID) family, members of which are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative manner by suppressing their heterodimerization partners through the HLH domains. This protein may play a role in negatively regulating cell differentiation. A pseudogene has been identified for this gene.[6] A research published by "Nature" in 01/2016, authored by italian researchers Antonio Iavarone and Anna Lasorella, from Columbia University, states that ID2 protein has a relevant role in the development and resistance to therapies of glioblastoma, the most aggressive of brain cancers.[7]
Interactions
ID2 has been shown to interact with MyoD[8] and NEDD9.[9]
See also
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000115738 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020644 - Ensembl, May 2017
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H, Oda K (Feb 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.
- ↑ "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".
- ↑ "An ID2-dependent mechanism for VHL inactivation in cancer".
- ↑ Langlands K, Yin X, Anand G, Prochownik EV (Aug 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. PMID 9242638. doi:10.1074/jbc.272.32.19785.
- ↑ Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA (Oct 1999). "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain". Exp. Cell Res. 252 (1): 224–35. PMID 10502414. doi:10.1006/excr.1999.4609.
Further reading
- Biggs J, Murphy EV, Israel MA (1992). "A human Id-like helix-loop-helix protein expressed during early development". Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1512–6. PMC 48481
. PMID 1741406. doi:10.1073/pnas.89.4.1512. - Iavarone A, Garg P, Lasorella A, Hsu J, Israel MA (1994). "The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein". Genes Dev. 8 (11): 1270–84. PMID 7926730. doi:10.1101/gad.8.11.1270.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298. doi:10.1016/0378-1119(94)90802-8.
- Kurabayashi M, Jeyaseelan R, Kedes L (1993). "Two distinct cDNA sequences encoding the human helix-loop-helix protein Id2". Gene. 133 (2): 305–6. PMID 8224921. doi:10.1016/0378-1119(93)90658-P.
- Mathew S, Chen W, Murty VV, Benezra R, Chaganti RS (1996). "Chromosomal assignment of human ID1 and ID2 genes". Genomics. 30 (2): 385–7. PMID 8586447. doi:10.1006/geno.1995.0037.
- Lasorella A, Iavarone A, Israel MA (1996). "Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins". Mol. Cell. Biol. 16 (6): 2570–8. PMC 231247 . PMID 8649364.
- Hara E, Hall M, Peters G (1997). "Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors". EMBO J. 16 (2): 332–42. PMC 1169639 . PMID 9029153. doi:10.1093/emboj/16.2.332.
- 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): 19785–93. PMID 9242638. doi:10.1074/jbc.272.32.19785.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3.
- 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. PMC 1171189 . PMID 10022839. doi:10.1093/emboj/18.4.968.
- Yokota Y, Mansouri A, Mori S, Sugawara S, Adachi S, Nishikawa S, Gruss P (1999). "Development of peripheral lymphoid organs and natural killer cells depends on the helix-loop-helix inhibitor Id2". Nature. 397 (6721): 702–6. PMID 10067894. doi:10.1038/17812.
- Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA (1999). "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain". Exp. Cell Res. 252 (1): 224–35. PMID 10502414. doi:10.1006/excr.1999.4609.
- Moldes M, Boizard M, Liepvre XL, Fève B, Dugail I, Pairault J (2000). "Functional antagonism between inhibitor of DNA binding (Id) and adipocyte determination and differentiation factor 1/sterol regulatory element-binding protein-1c (ADD1/SREBP-1c) trans-factors for the regulation of fatty acid synthase promoter in adipocytes". Biochem. J. 344 Pt 3 (Pt 3): 873–80. PMC 1220711 . PMID 10585876. doi:10.1042/0264-6021:3440873.
- Liu J, Shi W, Warburton D (2000). "A cysteine residue in the helix-loop-helix domain of Id2 is critical for homodimerization and function". Biochem. Biophys. Res. Commun. 273 (3): 1042–7. PMID 10891368. doi:10.1006/bbrc.2000.3055.
- Lasorella A, Noseda M, Beyna M, Yokota Y, Iavarone A (2000). "Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins". Nature. 407 (6804): 592–8. PMID 11034201. doi:10.1038/35036504.
- Roberts EC, Deed RW, Inoue T, Norton JD, Sharrocks AD (2001). "Id Helix-Loop-Helix Proteins Antagonize Pax Transcription Factor Activity by Inhibiting DNA Binding". Mol. Cell. Biol. 21 (2): 524–33. PMC 86614 . PMID 11134340. doi:10.1128/MCB.21.2.524-533.2001.
- Wang S, Sdrulla A, Johnson JE, Yokota Y, Barres BA (2001). "A role for the helix-loop-helix protein Id2 in the control of oligodendrocyte development". Neuron. 29 (3): 603–14. PMID 11301021. doi:10.1016/S0896-6273(01)00237-9.
- Wong J, Funes-Duran M, Ahlberg J, Round J, O'Connell R, Miller R, Chen E, Richmond PA, Vierra CA (2001). "Characterization of a basic helix-loop-helix protein, ABF-1: nuclear localization, transcriptional properties, and interaction with Id-2". DNA Cell Biol. 20 (8): 465–71. PMID 11560778. doi:10.1089/104454901316976091.
- Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y (2001). "Protein–Protein Interaction Panel Using Mouse Full-Length cDNAs". Genome Res. 11 (10): 1758–65. PMC 311163 . PMID 11591653. doi:10.1101/gr.180101.
External links
- ID2 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
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