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Id1

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Id1

Inhibitor of DNA binding 1, dominant negative helix-loop-helix protein
Identifiers
Symbols  ; ID; bHLHb24
External IDs ChEMBL: GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

DNA-binding protein inhibitor ID-1 is a protein that in humans is encoded by the ID1 gene.[1][2]

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

  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.  
  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.  
  3. ^ Ruzinova, M and Benezra, R (2003). "Id proteins in development, cell cycle and cancer". Trends in Cell Biology 13 (8): 410–8.  
  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.  
  5. ^ "Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein". 
  6. ^ Garkavtsev I, Kozin SV, Chernova O, Xu L, Winkler F, Brown E, Barnett GH, Jain RK (March 2004). "The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis". Nature 428 (6980): 328–32.  
  7. ^ 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.  
  8. ^ 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.  
  9. ^ 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.  
  10. ^ 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.  
  11. ^ Ling MT, Chiu YT, Lee TK, Leung SC, Fung MK, Wang X, Wong KF, Wong YC (September 2008). "Id-1 induces proteasome-dependent degradation of the HBX protein". J. Mol. Biol. 382 (1): 34–43.  
  12. ^ 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.  
  13. ^ 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". Biochem. Biophys. Res. Commun. 328 (2): 517–21.  
  14. ^ Lyden D, Young AZ, Zagzag D, Yan W, Gerald W, O'Reilly R, Bader BL, Hynes RO, Zhuang Y, Manova K, Benezra R (October 1999). "Id1 and Id3 are required for neurogenesis, angiogenesis and vascularization of tumour xenografts". Nature 401 (6754): 670–7.  
  15. ^ Lyden D, Hattori K, Dias S, Costa C, Blaikie P, Butros L, Chadburn A, Heissig B, Marks W, Witte L, Wu Y, Hicklin D, Zhu Z, Hackett NR, Crystal RG, Moore MA, Hajjar KA, Manova K, Benezra R, Rafii S (November 2001). "Impaired recruitment of bone-marrow-derived endothelial and hematopoietic precursor cells blocks tumor angiogenesis and growth". Nat. Med. 7 (11): 1194–201.  
  16. ^ Henke E, Perk J, Vider J, de Candia P, Chin Y, Solit DB, Ponomarev V, Cartegni L, Manova K, Rosen N, Benezra R (January 2008). "Peptide-conjugated antisense oligonucleotides for targeted inhibition of a transcriptional regulator in vivo". Nat. Biotechnol. 26 (1): 91–100.  
  17. ^ Mellick AS, Plummer PN, Nolan DJ, Gao D, Bambino K, Hahn M, Catena R, Turner V, McDonnell K, Benezra R, Brink R, Swarbrick A, Mittal V (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.  

Further reading

External links

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