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Gene Review

IGF2BP1  -  insulin-like growth factor 2 mRNA binding...

Homo sapiens

Synonyms: CRD-BP, CRDBP, Coding region determinant-binding protein, IGF-II mRNA-binding protein 1, IGF2 mRNA-binding protein 1, ...
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Disease relevance of IGF2BP1

  • IMP mRNA expression levels might play an important role in ovarian cancer development and progression, and IMP-1 overexpression is a prognostic marker for patients with ovarian cancer [1].
  • The mean value of the relative IMP-1 mRNA expression ratio was significantly higher in both ovarian cancer and adenoma samples compared to normal ovarian samples (p<0.05) [1].
  • The glioma lines also secreted various amounts of two smaller inhibitors of metalloproteinases (IMPs), also seen in rabbit brain capillary endothelial cell CM (IMP-1 at Mr 22,000 and IMP-2 at Mr 19,000), and an inhibitor not previously identified (IMP-3 at Mr 16,500) [2].
  • 8q24 Copy number gains and expression of the c-myc mRNA stabilizing protein CRD-BP in primary breast carcinomas [3].
  • The highest frequency (60%) of CRD-BP positive tumors was observed in meningiomas, either benign (11/18) or atypical (3/3) [4].

Psychiatry related information on IGF2BP1

  • Using this method, we found that the fragile X mental retardation protein (FMRP) isoform 18 and the human zipcode-binding protein 1 ortholog IMP1, an RNA transport factor, were present on common mRNAs [5].

High impact information on IGF2BP1

  • In contrast to most other organs, intestinal epithelial cells continue to express IMP1 postnatally, and Imp1(-/-) mice exhibited impaired development of the intestine, with small and misshapen villi and twisted colon crypts [6].
  • Taken together, the results demonstrate that IMP1 is essential for normal growth and development [6].
  • However, it was unclear why a CRD-BP is required to protect a well-translated mRNA whose coding region is covered with ribosomes [7].
  • CRD-BP/IMP1 expression characterizes cord blood CD34+ stem cells and affects c-myc and IGF-II expression in MCF-7 cancer cells [8].
  • CRD-BP/IMP1 was detected only in cord blood-derived CD34(+) stem cells and not in any other cell type of either adult or cord blood origin [8].

Chemical compound and disease context of IGF2BP1

  • Imipenem-resistant Pseudomonas aeruginosa producing IMP-1 metallo-beta-lactamases and lacking the outer-membrane protein OprD [9].

Biological context of IGF2BP1

  • Furthermore, by applying the short interfering RNA methodology in MCF-7 cells, we observed, subsequent to knocking down CRD-BP/IMP1, decreased c-myc expression, increased IGF-II mRNA levels, and reduced cell proliferation rates [8].
  • The c-myc mRNA coding region determinant-binding protein (CRD-BP) was first identified as a masking protein that stabilizes c-myc mRNA in a cell-free mRNA degradation system [10].
  • By using K562 leukemia cells as a model, we show that CRD-BP gene silencing by RNA interference significantly promoted proliferation, indicating an inhibitory effect of CRD-BP on proliferation [10].
  • The coding region determinant binding protein (CRD-BP) was isolated by virtue of its high affinity to the c-myc mRNA coding region stability determinant and shown to shield this message from nucleolytic attack, prolonging its half-life [3].
  • CRD-BP expression was detected in 58.5% (69/118) of tumors, implying mechanisms of activation alternative to gene amplification [3].

Anatomical context of IGF2BP1

  • Adult BM CD34(+) cells cultured in the presence of 5'-azacytidine expressed de novo CRD-BP/IMP1, suggesting that epigenetic modifications may be responsible for its silencing in adult non-expressing cells [8].
  • Thus, we have identified a dominant function for CRD-BP in cell proliferation of human K562 cells, involving a possible IGF-II-dependent mechanism that appears independent of its ability to serve as a c-myc mRNA masking protein [10].
  • Here, we confirm that human CRD-BP/IMP-1 binds to c-myc mRNA and that it is predominantly expressed in fetal tissues [11].
  • Moreover, hCRD-BP/IMP-1 expression was detected in cell lines of neoplastic origin and in selected primary tumors [11].
  • The ZBP1 then forms a ribonucleoprotein particle and moves in a myosin-dependent fashion by using the cytoskeleton for directional transport [12].

Associations of IGF2BP1 with chemical compounds

  • Significant associations were detected between CRD-BP expression and the absence of estrogen receptors (p = 0.005) and between the presence of 8q24 gains and an increased number of genomic changes as measured by CGH (p = 0.0017) [3].
  • 2. Venlafaxine was baseline resolved in its enantiomers using gamma-CD or HP-beta-CD, while imp1 (Wy45494) was baseline resolved using alpha-CD [13].
  • Because IMP-1 has been found in several clinically important carbapenem-resistant pathogens, there is a need for inhibitors of this enzyme that could protect broad spectrum antibiotics such as imipenem from hydrolysis and thus extend their utility [14].
  • Determination of high resolution crystal structures and molecular modeling of succinic acid inhibitor complexes with IMP-1 has allowed an understanding of the potency, stereochemistry, and structure-activity relationships of these inhibitors [14].
  • Previously, we have discovered that mutations G262S (yielding IMP-1) and G262A in IMP-6 stabilize the Zn(II) ligand His263 and thus the enzyme-substrate intermediate complex through a domino effect, which enhances conversion of drugs like ceftazidime, penicillins, and imipenem [15].

Physical interactions of IGF2BP1

  • CRD-BP has been assigned a role in stabilizing c-myc mRNA by preventing its endonucleolytic cleavage and in repressing the translation of the leader 3 IGF-II mRNA, the major embryonic species of this message [16].

Regulatory relationships of IGF2BP1


Other interactions of IGF2BP1

  • IMP-3 and IMP-1, two members of the IMP family with significant structural similarity, appear to have some distinct RNA targets and functions in K562 cells [17].
  • The IMP-12 enzyme is quite divergent from other IMP variants: its closest relatives are IMP-8 and IMP-2 (89 and 88% sequence identity, respectively), and IMP-1 is 85% identical to IMP-12 [18].
  • To our knowledge this is the first observation of a direct translational role of G3BP1 for any mRNA and the first report of a translation inhibition by IMP1 and HuD on the tau mRNA in a cell system [19].
  • CRD-BP: a c-Myc mRNA stabilizing protein with an oncofetal pattern of expression [16].
  • The coding region determinant-binding protein (CRD-BP) is an RNA binding protein that recognizes c-myc and IGF-II leader 3 mRNAs as well as the oncofetal H19 RNA [4].

Analytical, diagnostic and therapeutic context of IGF2BP1

  • Log-rank testing showed that IMP-1 overexpression (p=0.0398) and an advanced clinical stage (p=0.0050) were significantly correlated with poor patient survival, whereas neither IMP-2 nor IMP-3 overexpression were associated with poor prognoses [1].
  • Of these 431 strains, 357 were found by PCR to carry genes for IMP-1 type MBL (bla(IMP-1)), while only 7 and 67 strains carried the IMP-2 gene (bla(IMP-2)) and the VIM-2 gene (bla(VIM-2)), respectively [20].
  • In this study, we used an electrophoretic mobility-shift assay in combination with equilibrium and kinetic analyses to characterize the assembly of the human zipcode-binding protein IMP1 on targets in the 3'-UTR from Igf-II mRNA and in H19 RNA [21].
  • To analyse CRD-BP expression in human cancer tissue, paired extracts of cancer and normal colon specimens from 21 patients were analysed by immunoblotting and/or reverse transcriptase-polymerase chain reaction [22].
  • In this study, 29 amino acid residue positions in and near the active-site pocket of the IMP-1 enzyme were randomized individually by site-directed mutagenesis of the corresponding codons in the bla(IMP-1) gene [23].


  1. Increased expression of IGF II mRNA-binding protein 1 mRNA is associated with an advanced clinical stage and poor prognosis in patients with ovarian cancer. Gu, L., Shigemasa, K., Ohama, K. Int. J. Oncol. (2004) [Pubmed]
  2. Expression of metalloproteinases and metalloproteinase inhibitors by fetal astrocytes and glioma cells. Apodaca, G., Rutka, J.T., Bouhana, K., Berens, M.E., Giblin, J.R., Rosenblum, M.L., McKerrow, J.H., Banda, M.J. Cancer Res. (1990) [Pubmed]
  3. 8q24 Copy number gains and expression of the c-myc mRNA stabilizing protein CRD-BP in primary breast carcinomas. Ioannidis, P., Mahaira, L., Papadopoulou, A., Teixeira, M.R., Heim, S., Andersen, J.A., Evangelou, E., Dafni, U., Pandis, N., Trangas, T. Int. J. Cancer (2003) [Pubmed]
  4. Expression of the RNA-binding protein CRD-BP in brain and non-small cell lung tumors. Ioannidis, P., Kottaridi, C., Dimitriadis, E., Courtis, N., Mahaira, L., Talieri, M., Giannopoulos, A., Iliadis, K., Papaioannou, D., Nasioulas, G., Trangas, T. Cancer Lett. (2004) [Pubmed]
  5. Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs. Rackham, O., Brown, C.M. EMBO J. (2004) [Pubmed]
  6. Dwarfism and impaired gut development in insulin-like growth factor II mRNA-binding protein 1-deficient mice. Hansen, T.V., Hammer, N.A., Nielsen, J., Madsen, M., Dalbaeck, C., Wewer, U.M., Christiansen, J., Nielsen, F.C. Mol. Cell. Biol. (2004) [Pubmed]
  7. Regulation of c-myc mRNA decay by translational pausing in a coding region instability determinant. Lemm, I., Ross, J. Mol. Cell. Biol. (2002) [Pubmed]
  8. CRD-BP/IMP1 expression characterizes cord blood CD34+ stem cells and affects c-myc and IGF-II expression in MCF-7 cancer cells. Ioannidis, P., Mahaira, L.G., Perez, S.A., Gritzapis, A.D., Sotiropoulou, P.A., Kavalakis, G.J., Antsaklis, A.I., Baxevanis, C.N., Papamichail, M. J. Biol. Chem. (2005) [Pubmed]
  9. Imipenem-resistant Pseudomonas aeruginosa producing IMP-1 metallo-beta-lactamases and lacking the outer-membrane protein OprD. Wang, C.X., Mi, Z.H. J. Med. Microbiol. (2006) [Pubmed]
  10. Targeted knockdown of the RNA-binding protein CRD-BP promotes cell proliferation via an insulin-like growth factor II-dependent pathway in human K562 leukemia cells. Liao, B., Patel, M., Hu, Y., Charles, S., Herrick, D.J., Brewer, G. J. Biol. Chem. (2004) [Pubmed]
  11. C-MYC and IGF-II mRNA-binding protein (CRD-BP/IMP-1) in benign and malignant mesenchymal tumors. Ioannidis, P., Trangas, T., Dimitriadis, E., Samiotaki, M., Kyriazoglou, I., Tsiapalis, C.M., Kittas, C., Agnantis, N., Nielsen, F.C., Nielsen, J., Christiansen, J., Pandis, N. Int. J. Cancer (2001) [Pubmed]
  12. Real-time visualization of ZBP1 association with beta-actin mRNA during transcription and localization. Oleynikov, Y., Singer, R.H. Curr. Biol. (2003) [Pubmed]
  13. Analysis of venlafaxine by capillary zone electrophoresis. Fanali, S., Cotichini, V., Porrà, R. Journal of capillary electrophoresis. (1997) [Pubmed]
  14. Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase. Toney, J.H., Hammond, G.G., Fitzgerald, P.M., Sharma, N., Balkovec, J.M., Rouen, G.P., Olson, S.H., Hammond, M.L., Greenlee, M.L., Gao, Y.D. J. Biol. Chem. (2001) [Pubmed]
  15. Hydroxyl Groups in the betabeta Sandwich of Metallo-beta-lactamases Favor Enzyme Activity: Tyr218 and Ser262 Pull Down the Lid. Oelschlaeger, P., Pleiss, J. J. Mol. Biol. (2007) [Pubmed]
  16. CRD-BP: a c-Myc mRNA stabilizing protein with an oncofetal pattern of expression. Ioannidis, P., Mahaira, L., Papadopoulou, A., Teixeira, M.R., Heim, S., Andersen, J.A., Evangelou, E., Dafni, U., Pandis, N., Trangas, T. Anticancer Res. (2003) [Pubmed]
  17. The RNA-binding protein IMP-3 is a translational activator of insulin-like growth factor II leader-3 mRNA during proliferation of human K562 leukemia cells. Liao, B., Hu, Y., Herrick, D.J., Brewer, G. J. Biol. Chem. (2005) [Pubmed]
  18. IMP-12, a new plasmid-encoded metallo-beta-lactamase from a Pseudomonas putida clinical isolate. Docquier, J.D., Riccio, M.L., Mugnaioli, C., Luzzaro, F., Endimiani, A., Toniolo, A., Amicosante, G., Rossolini, G.M. Antimicrob. Agents Chemother. (2003) [Pubmed]
  19. Dynamic association with polysomes during P19 neuronal differentiation and an untranslated-region-dependent translation regulation of the tau mRNA by the tau mRNA-associated proteins IMP1, HuD, and G3BP1. Atlas, R., Behar, L., Sapoznik, S., Ginzburg, I. J. Neurosci. Res. (2007) [Pubmed]
  20. PCR typing of genetic determinants for metallo-beta-lactamases and integrases carried by gram-negative bacteria isolated in Japan, with focus on the class 3 integron. Shibata, N., Doi, Y., Yamane, K., Yagi, T., Kurokawa, H., Shibayama, K., Kato, H., Kai, K., Arakawa, Y. J. Clin. Microbiol. (2003) [Pubmed]
  21. Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability. Nielsen, J., Kristensen, M.A., Willemoës, M., Nielsen, F.C., Christiansen, J. Nucleic Acids Res. (2004) [Pubmed]
  22. Overexpression of an mRNA-binding protein in human colorectal cancer. Ross, J., Lemm, I., Berberet, B. Oncogene (2001) [Pubmed]
  23. Analysis of the context dependent sequence requirements of active site residues in the metallo-beta-lactamase IMP-1. Materon, I.C., Beharry, Z., Huang, W., Perez, C., Palzkill, T. J. Mol. Biol. (2004) [Pubmed]
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