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Gene Review

Imp  -  IGF-II mRNA-binding protein

Drosophila melanogaster

Synonyms: CG1691, Dmel\CG1691, IGF-II, IGF2BP1, IMP, ...
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High impact information on Imp


Biological context of Imp

  • We found that each Imp-alpha is expressed during a specific and limited period of spermatogenesis [5].
  • These data indicate that each Imp-alpha protein carries during Drosophila spermatogenesis distinct, albeit overlapping, functions that may involve nuclear import of proteins, microtubule organisation, and other yet unknown processes [5].
  • We find that these KH domain mutations result in partial loss of function or no significant loss of function for the phenotypes assayed [6].
  • Using a construct containing only the RNA binding domain of PSI (PSI-KH03), we introduced a physiologically relevant point mutation into each KH domain of PSI individually and measured stability and RNA binding affinity of the resulting mutant proteins [7].
  • Deletion of the C-terminus, which contains a part of the KH domain, alleviated apoptosis by the H-ERA mutant, suggesting the importance of this domain in the function of H-ERA [8].

Anatomical context of Imp


Analytical, diagnostic and therapeutic context of Imp

  • We have sequenced the Drosophila homologue (dIMP) of these genes, and examined its expression pattern in Drosophila embryos by in situ hybridization [9].


  1. Modulation of P-element pre-mRNA splicing by a direct interaction between PSI and U1 snRNP 70K protein. Labourier, E., Adams, M.D., Rio, D.C. Mol. Cell (2001) [Pubmed]
  2. Imp Associates with Squid and Hrp48 and Contributes to Localized Expression of gurken in the Oocyte. Geng, C., Macdonald, P.M. Mol. Cell. Biol. (2006) [Pubmed]
  3. MASK, a large ankyrin repeat and KH domain-containing protein involved in Drosophila receptor tyrosine kinase signaling. Smith, R.K., Carroll, P.M., Allard, J.D., Simon, M.A. Development (2002) [Pubmed]
  4. A novel KH-domain protein mediates cell adhesion processes in Drosophila. Lo, P.C., Frasch, M. Dev. Biol. (1997) [Pubmed]
  5. Patterns of importin-alpha expression during Drosophila spermatogenesis. Giarrè, M., Török, I., Schmitt, R., Gorjánácz, M., Kiss, I., Mechler, B.M. J. Struct. Biol. (2002) [Pubmed]
  6. Substitution of Critical Isoleucines in the KH Domains of Drosophila Fragile X Protein Results in Partial Loss-of-Function Phenotypes. Banerjee, P., Nayar, S., Hebbar, S., Fox, C.F., Jacobs, M.C., Park, J.H., Fernandes, J.J., Dockendorff, T.C. Genetics (2007) [Pubmed]
  7. Distinct contributions of KH domains to substrate binding affinity of Drosophila P-element somatic inhibitor protein. Chmiel, N.H., Rio, D.C., Doudna, J.A. RNA (2006) [Pubmed]
  8. Mammalian homologue of E. coli Ras-like GTPase (ERA) is a possible apoptosis regulator with RNA binding activity. Akiyama, T., Gohda, J., Shibata, S., Nomura, Y., Azuma, S., Ohmori, Y., Sugano, S., Arai, H., Yamamoto, T., Inoue, J. Genes Cells (2001) [Pubmed]
  9. The biphasic expression of IMP/Vg1-RBP is conserved between vertebrates and Drosophila. Nielsen, J., Cilius Nielsen, F., Kragh Jakobsen, R., Christiansen, J. Mech. Dev. (2000) [Pubmed]
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