Physical and functional interaction of the HECT ubiquitin-protein ligases E6AP and HERC2

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Journal of Biological Chemistry. 2011, 286(22), pp. 19410-19416. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M110.205211
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Deregulation of the ubiquitin-protein ligase E6AP contributes to the development of the Angelman syndrome and to cervical carcinogenesis suggesting that the activity of E6AP needs to be under tight control. However, how E6AP activity is regulated at the post-translational level under non-pathologic conditions is poorly understood. In this study, we report that the giant protein HERC2, which is like E6AP a member of the HECT family of ubiquitin-protein ligases, binds to E6AP. The interaction is mediated by the RCC1-like domain 2 of HERC2 and a region spanning amino acid residues 150-200 of E6AP. Furthermore, we provide evidence that HERC2 stimulates the ubiquitin-protein ligase activity of E6AP in vitro and within cells and that this stimulatory effect does not depend on the ubiquitin-protein ligase activity of HERC2. Thus, the data obtained indicate that HERC2 acts as a regulator of E6AP.

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ISO 690KÜHNLE, Simone, Ulrike KOGEL, Sandra GLOCKZIN, Andreas MARQUARDT, Aaron CIECHANOVER, Konstantin MATENTZOGLU, Martin SCHEFFNER, 2011. Physical and functional interaction of the HECT ubiquitin-protein ligases E6AP and HERC2. In: Journal of Biological Chemistry. 2011, 286(22), pp. 19410-19416. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M110.205211
BibTex
@article{Kuhnle2011-06-03Physi-16761,
  year={2011},
  doi={10.1074/jbc.M110.205211},
  title={Physical and functional interaction of the HECT ubiquitin-protein ligases E6AP and HERC2},
  number={22},
  volume={286},
  issn={0021-9258},
  journal={Journal of Biological Chemistry},
  pages={19410--19416},
  author={Kühnle, Simone and Kogel, Ulrike and Glockzin, Sandra and Marquardt, Andreas and Ciechanover, Aaron and Matentzoglu, Konstantin and Scheffner, Martin}
}
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