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Gene Review

drk  -  downstream of receptor kinase

Drosophila melanogaster

Synonyms: 24/1, CG6033, DRK, Dmel\CG6033, Downstream of receptor kinase, ...
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High impact information on drk

  • Here we report that another gene, E(sev)2B, required for proper signaling by sevenless encodes a protein of the structure SH3-SH2-SH3 [1].
  • These results suggest that drk binds autophosphorylated receptor tyrosine kinases with its SH2 domain and the Sos GNRP through its SH3 domains, thereby coupling receptor tyrosine kinases to Ras activation [2].
  • Drk biological activity correlates with binding of its SH2 domain to activated receptor tyrosine kinases and concomitant localization of drk to the plasma membrane [2].
  • Genetic analysis suggests that drk function is essential for signaling by the sevenless receptor tyrosine kinase [2].
  • In Caenorhabditis elegans and Drosophila, genetic studies have shown that Ras activation by tyrosine kinases requires the protein Sem-5/drk, which contains a single Src-homology (SH) 2 domain and two flanking SH3 domains [3].

Biological context of drk

  • Protein folding kinetic data have been obtained for the marginally stable N-terminal Src homology 3 domain of the Drosophila protein drk (drkN SH3) in an investigation of the hydrodynamic properties of its folding transition state [4].
  • The testicular phenotypes were suppressed by heterozygous hypomorphic mutations in the Dras1 and drk genes, indicating cross talk between RacGAP-regulated signaling and that of the Ras pathway [5].
  • The isolated N-terminal Src homology 3 (SH3) domain of Drosophila drk exists in equilibrium between folded and unfolded states in aqueous buffer near neutral pH [6].

Associations of drk with chemical compounds

  • Measurements of 15N NMR relaxation parameters have been used to characterize the backbone dynamics of folded and denatured states of the N-terminal SH3 domain from the adapter protein drk, in high salt or guanidinium chloride, respectively [7].

Other interactions of drk

  • CSW also serves as an adaptor protein for DRK binding, physically linking Torso to Ras activation [8].

Analytical, diagnostic and therapeutic context of drk

  • The presence of residual structure in the unfolded state of the N-terminal SH3 domain of Drosophila drk (drkN SH3 domain) has been investigated using far- and near-UV circular dichroism (CD), fluorescence, and NMR spectroscopy [9].
  • Residue-specific pK(a) values of side-chain carboxyl groups are presented for the first time for an unfolded protein (drk U(exch) state), determined from a pH titration [10].


  1. An SH3-SH2-SH3 protein is required for p21Ras1 activation and binds to sevenless and Sos proteins in vitro. Simon, M.A., Dodson, G.S., Rubin, G.M. Cell (1993) [Pubmed]
  2. A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos. Olivier, J.P., Raabe, T., Henkemeyer, M., Dickson, B., Mbamalu, G., Margolis, B., Schlessinger, J., Hafen, E., Pawson, T. Cell (1993) [Pubmed]
  3. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Rozakis-Adcock, M., Fernley, R., Wade, J., Pawson, T., Bowtell, D. Nature (1993) [Pubmed]
  4. Characterization of the hydrodynamic properties of the folding transition state of an SH3 domain by magnetization transfer NMR spectroscopy. Tollinger, M., Neale, C., Kay, L.E., Forman-Kay, J.D. Biochemistry (2006) [Pubmed]
  5. RotundRacGAP functions with Ras during spermatogenesis and retinal differentiation in Drosophila melanogaster. Bergeret, E., Pignot-Paintrand, I., Guichard, A., Raymond, K., Fauvarque, M.O., Cazemajor, M., Griffin-Shea, R. Mol. Cell. Biol. (2001) [Pubmed]
  6. Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer. Zhang, O., Forman-Kay, J.D. Biochemistry (1995) [Pubmed]
  7. Characterization of the backbone dynamics of folded and denatured states of an SH3 domain. Farrow, N.A., Zhang, O., Forman-Kay, J.D., Kay, L.E. Biochemistry (1997) [Pubmed]
  8. Opposing actions of CSW and RasGAP modulate the strength of Torso RTK signaling in the Drosophila terminal pathway. Cleghon, V., Feldmann, P., Ghiglione, C., Copeland, T.D., Perrimon, N., Hughes, D.A., Morrison, D.K. Mol. Cell (1998) [Pubmed]
  9. Cooperative interactions and a non-native buried Trp in the unfolded state of an SH3 domain. Crowhurst, K.A., Tollinger, M., Forman-Kay, J.D. J. Mol. Biol. (2002) [Pubmed]
  10. Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy. Tollinger, M., Forman-Kay, J.D., Kay, L.E. J. Am. Chem. Soc. (2002) [Pubmed]
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