[HTML][HTML] 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
R Mouchantaf, BA Azakir, PS McPherson… - Journal of Biological …, 2006 - ASBMB
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 vivo through coimmunoprecipation. Itch and FAM …
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 vivo through coimmunoprecipation. Itch and FAM …
