ID1

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Inhibitor of DNA binding 1, dominant negative helix-loop-helix protein
Identifiers
Symbols ID1; ID; bHLHb24
External IDs OMIM600349 MGI96396 HomoloGene1631 GeneCards: ID1 Gene
RNA expression pattern
PBB GE ID1 208937 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3397 15901
Ensembl ENSG00000125968 ENSMUSG00000042745
UniProt P41134 P20067
RefSeq (mRNA) NM_002165.3 NM_010495.2
RefSeq (protein) NP_002156.2 NP_034625.1
Location (UCSC) Chr 20:
30.19 – 30.19 Mb
Chr 2:
152.56 – 152.56 Mb
PubMed search [1] [2]

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

  1. ^ 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. 
  2. ^ 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. 
  3. ^ 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. 
  4. ^ 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. 
  5. ^ "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. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ 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. 
  9. ^ 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. 
  10. ^ 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. 
  11. ^ 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. 
  12. ^ 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. 
  13. ^ 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. 
  14. ^ 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. 
  15. ^ 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. 
  16. ^ 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. 
  17. ^ 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

[edit] External links

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


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