The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X.

@article{Mouchantaf2006TheUL,
  title={The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X.},
  author={Rania Mouchantaf and Bilal A. Azakir and Peter S McPherson and Susan M Millard and Stephen A Wood and Annie Angers},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 50},
  pages={38738-47}
}
Itch is a ubiquitin ligase that has been implicated in the regulation of a number of cellular processes. We previously have identified Itch as a binding partner for the endocytic protein Endophilin and found it to be localized to endosomes. Using affinity purification coupled to mass spectrometry, we have now identified the ubiquitin-protease FAM/USP9X as a binding partner of Itch. The association between Itch and FAM/USP9X was confirmed in vitro by glutathione S-transferase pulldown and in… CONTINUE READING

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Itch self-polyubiquitylation occurs through lysine-63 linkages.

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1717–1722 FAM Protects the Ubiquitin Ligase Itch 38746 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

E. Gallagher, M. Gao, Y. C. Liu, M. Karin
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451–455 FAM Protects the Ubiquitin Ligase

Wood, Annie Angers Rania Mouchantaf, +3 authors A Stephen
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